Assessment of Antiviral Activities of Four Licorice Compounds against Zucchini Yellow Mosaic Virus through Molecular Docking

Assessment of Antiviral Activities of Four Licorice Compounds against Zucchini Yellow Mosaic Virus through Molecular Docking | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Assessment of Antiviral Activities of Four Licorice Compounds against Zucchini Yellow Mosaic Virus through Molecular Docking Shrouk E.E. Farag, Shafik D. Ibrahim, Atef S. Sadik, Mamdouh H. Abdel-Gaffar This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-7011143/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract This study investigates the molecular docking and binding affinities of four licorice-derived bioactive compounds against 10 proteins of Zucchini yellow mosaic virus (ZYMV), including P1, HC-Pro, P3, 6K1, 6K2, CI, NIa-VPg, NIa-Pro, and NIb. ZYMV is a significant viral pathogen affecting cucurbit crops worldwide, leading to major economic losses. Traditional antiviral strategies have limitations, and bioactive compounds derived from plants have gained attention for their potential to inhibit viral activity. The docking scores reveal that Glycyrrhetic acid and Liquiritin demonstrate the strongest binding, particularly to the P1 target, while Isoliquiritin shows weaker binding. Acyclovir, the control drug, exhibited the least effective binding across all targets. The bonding interactions between the compounds and ZYMV proteins involve a combination of hydrophobic (alkyl, Pi-Alkyl, Pi-Sigma), electrostatic (hydrogen bonds, Pi-Cation, Pi-Anion), and aromatic (Pi-Pi) interactions, each contributing to the stability of the protein-ligand complexes. Glycyrrhetic acid and Liquiritin primarily engage in hydrophobic interactions, enhancing their binding stability, while Isoliquiritin and Glabridin also form electrostatic and aromatic interactions. Some unfavorable interactions, such as donor-donor or acceptor-acceptor bonds, were identified, indicating potential regions for optimization in ligand binding. These findings highlight the promising antiviral potential of licorice-derived compounds, particularly Glycyrrhetic acid and Liquiritin, as inhibitors of ZYMV. The results emphasize the role of non-polar interactions in stabilizing the binding complexes, suggesting these compounds could modulate protein function. The study provides valuable insights for future antiviral drug development, with potential strategies to optimize binding affinity and enhance the efficacy of licorice-derived bioactive compounds in targeting ZYMV. Antiviral drug development Binding affinity Licorice Molecular docking Protein-ligand interactions ZYMV Introduction Zucchini Yellow Mosaic Virus (ZYMV) is a significant viral pathogen affecting cucurbit crops, particularly zucchini, leading to substantial yield losses worldwide [1]. Transmitted by aphids, ZYMV causes symptoms such as yellowing of leaves, mosaic patterns, and stunted growth, severely impacting crop quality and yield [2]. Traditional control measures, including chemical pesticides and resistant cultivars, are often ineffective, environmentally damaging, or economically unsustainable [3, 4]. This has prompted an increased interest in exploring alternative, eco-friendly solutions for managing viral diseases in crops [5, 6]. Licorice ( Glycyrrhiza glabra ), a plant renowned for its medicinal properties, has shown potential as a source of antiviral agents. Its bioactive compounds, including glycyrrhizin, flavonoids, and triterpenoids, are known for their antiviral, anti-inflammatory, and immune-modulating activities [7]. These compounds have demonstrated effectiveness against a variety of human and plant viruses [8-10]. Recent advancements in computational tools, particularly molecular docking, have enabled researchers to predict and analyze the interactions between bioactive compounds and viral proteins. Molecular docking offers a powerful, cost-effective method to screen potential antiviral agents by simulating the binding of compounds to critical viral proteins, such as the coat protein (CP) and RNA-dependent RNA polymerase (RdRp), which play key roles in the replication and infectivity of plant viruses [11-14]. Molecular docking has become an invaluable tool in the study of plant viruses, particularly in the identification of potential antiviral compounds. By simulating the interactions between small molecules and viral proteins, molecular docking allows researchers to predict how these compounds may inhibit viral replication, thus offering a promising alternative to traditional experimental approaches [15, 16]. This technique allows for the identification of compounds with strong binding affinities to viral proteins, suggesting their potential for inhibiting viral replication [17]. This computational technique is especially useful in the context of plant viruses, where effective antiviral agents are limited [18]. It enables the identification of key viral proteins, such as coat proteins or RNA-dependent RNA polymerases, which are critical for the virus’s replication and infectivity [19]. Docking studies can also reveal the precise binding sites and interactions between bioactive compounds-often derived from plants themselves-and these viral proteins [20]. Molecular docking studies have revealed that ASP 121, ASN 48, and TYR 38 are key sites of interaction between the PVY HC-Pro C-terminal domain and these compounds. These amino acid residues are critical for the design and synthesis of novel urea derivatives as potential antiviral agents [21]. This in silico approach enables the identification of promising compounds from licorice that could inhibit viral replication and reduce the severity of disease symptoms in infected crops. The objective of this study is to evaluate the antiviral activities of four licorice-derived compounds-glycyrrhizin, liquiritigenin, isoliquiritigenin, and glabridin-against ZYMV using molecular docking analysis. Through this computational approach, we aim to identify the most promising compounds that could be further explored for the development of antiviral agents against ZYMV. The findings from this study could contribute to the development of more sustainable and effective strategies for managing viral diseases in cucurbit crops. Materials and Methods Selected compounds for docking analysis Four bioactive compounds (Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin) derived from Licorice were selected for assessment their antiviral activities against the proteins encoded from the ten genes of the genome of an Egyptian strain of ZYMV documented in GenBank under accession number of LC795783.1 using molecular docking tool. Their chemical structures were retrieved in 2D SDF format from the PubChem database [https://pubchem.ncbi.nlm.nih.gov/]. Preparation of ZYMV Proteins The ZYMV proteins [P1 (Accession: BFF82028.1), HC-Pro (Accession: BFF82029.1), P3 (Accession: BFF82030.1), 6k1 (Accession: BFF82031.1), CI (Accession: BFF82032.1), 6K2 (Accession: BFF82033.1), NIa-VPg (Accession: BFF82034.1), NIb-Pro (Accession: BFF82035.1), NIb (Accession: BFF82036.1), and CP (Accession: BFF82037.1)] were retrieved in FASTA format from the NCBI database [https://www.ncbi.nlm.nih.gov]. To obtain the 3D structures of the target proteins in PDB format, a search was performed on the Protein Data Bank (PDB) website [https://www.rcsb.org/]. In cases where the structures were unavailable, 3D models of the proteins were generated through homology modeling, using sequence alignments to known structures, with tools such as SWISS-MODEL or Phyre2. Virtual Screening of Bioactive Compounds A library of bioactive compounds was compiled for virtual screening. The screening was conducted using PyRx software [https://sourceforge.net/projects/pyrx/], which combines energy minimization with docking simulations through the AutoDock Vina plugin. The compounds were docked against the replicase and coat protein of PVX to prioritize those exhibiting lower binding energy values, suggesting stronger binding potential. The 2D molecular structures were converted to 3D forms and optimized for energy minimization using tools like Open Babel and Chem3D. Molecular Docking The docking process involved several preparatory steps. Target proteins were processed by removing water molecules and irrelevant ligands using PyMOL. Hydrogen atoms were added, and either Kollman or Gasteiger charges were assigned to the protein. The ligands were energy-minimized using Open Babel or Chem3D to ensure optimal geometry for the docking process. Docking simulations were carried out with CB-Dock and AutoDock Vina. The binding affinities (in kcal/mol) of each protein-ligand complex were recorded. CB-Dock facilitated the automatic identification of potential binding sites, ensuring more accurate docking results. Visualization and Analysis The results of the docking simulations were analyzed and visualized using Discovery Studio 2022 [https://10.0.142.116/Pharmaceutical-Sciences.543] to examine key interactions such as hydrogen bonds, hydrophobic contacts, and ionic interactions between the protein and the ligands. Results The data presented in Table 1 provides insights into the molecular docking and binding affinities of four licorice-derived bioactive compounds-Glabridin, Glycyrrhetic acid, Isoliquiritin, and Liquiritin-against various ZYMV protein targets, including P1, HC-Pro, P3, and others. The table also compares these compounds to the control drug, Acyclovir. Glabridin shows moderate binding across all targets, with docking scores ranging from -6.3 to -8.8. This suggests that Glabridin can effectively bind to the ZYMV protein targets, though it may not exhibit the strongest binding compared to the other compounds. Glycyrrhetic acid demonstrates relatively consistent docking scores, ranging from -6.1 to -9.4, indicating favorable binding with most ZYMV protein targets. It achieves the lowest docking score against the P1 target (-9.4), suggesting strong binding in this case. Isoliquiritin shows docking scores ranging from -5.8 to -8.7, indicating a weaker binding profile overall. Its best binding score is with the NIa-VPg target (-8.7), but it also demonstrates relatively weaker interactions with other targets like P3 (-6.2) and 6K1 (-5.8). Liquiritin presents docking scores ranging from -6.1 to -9.6, indicating promising binding interactions across multiple targets. Its best interaction is seen with the P1 target (-9.6), similar to Glycyrrhetic acid, highlighting its strong potential as a ZYMV inhibitor. Acyclovir, the control drug, shows generally weaker docking scores compared to the licorice compounds, with values ranging from -3.8 to -6.3, indicating that it binds less effectively to the ZYMV proteins compared to the licorice compounds. The data presented (Table 2 & Fig. 1) reveals the variety of bonding interactions that occur between the ligands and the amino acid residues of the protein. Conventional hydrogen bonds are the most common form of interaction, helping to stabilize the protein-ligand complexes. Alkyl and Pi-Alkyl interactions also feature prominently, highlighting the role of hydrophobic and aromatic stacking interactions in binding affinity. In some cases, the dataset points to unfavorable interactions, such as donor-donor and acceptor-acceptor bonds, which could inform future modifications to improve ligand binding or optimize the overall interaction profile. These unfavorable interactions might also provide insight into areas where ligand optimization could be beneficial to enhance stability or specificity in targeting the protein. The presence of diverse bonding types, including hydrogen, alkyl, and pi-based interactions, reflects the complex nature of protein-ligand binding and offers valuable information for understanding how these bioactive compounds interact with the ZYMV-P1 protein. This analysis could inform future research on drug design, specifically in targeting ZYMV or similar viruses, and may even contribute to the development of more effective antiviral compounds based on licorice-derived molecules. Overall, the title and the associated results emphasize the importance of understanding the molecular interactions that underlie potential therapeutic interventions. The results presented in Table (3 & Fig. 2) highlight the bonding interactions between various amino acid residues in the ZYMV-HC-Pro protein and four licorice-derived bioactive compounds: Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin. The data reveals a diverse array of interaction types, including conventional hydrogen bonds, alkyl interactions, pi-stacking, and more specialized bonds like Pi-Anion and Pi-Sulfur interactions. For Glycyrrhetic acid , the interactions are primarily hydrophobic, with alkyl bonds playing a significant role in stabilizing the complex at sites such as CYS A:342, ALA A:337, and ILE A:417. Conventional hydrogen bonds are also present at TYR A:335, reinforcing the structural integrity of the binding. The presence of multiple alkyl interactions at ALA A:337, in particular, indicates a strong hydrophobic environment, likely contributing to the stabilization of the ligand within the protein’s binding site. In the case of Isoliquiritin , several notable pi-based interactions are observed, such as the Pi-Alkyl interaction at VAL A:352, which suggests a strong aromatic interaction, likely aiding the binding affinity. TYR A:335, ALA A:349, and LEU A:430 exhibit conventional hydrogen bonds, contributing to a stable protein-ligand interface. Additionally, GLU A:401 shows a more complex bonding pattern, involving conventional hydrogen bonds, as well as Pi-Anion and Pi-Sigma interactions, which could indicate a more sophisticated interaction mode with this ligand. For Liquiritin , the interaction profile is again diverse, with conventional hydrogen bonds predominating, such as those at TYR A:335, GLY A:456, and VAL A:416. Interestingly, HIS A:415 shows an unfavorable donor-donor interaction, which could suggest potential areas where the binding is less stable or where further ligand optimization might improve affinity. Furthermore, CYS A:342 engages in a Pi-Sulfur interaction, which is notable for its role in stabilizing the ligand through sulfur-aromatic interactions, commonly seen in enzyme-inhibitor complexes. ILE A:417 also exhibits a Pi-Sigma interaction, further highlighting the contribution of aromatic stacking in binding. Finally, Glabridin shows a combination of both conventional hydrogen bonds and more specialized interactions. For example, SER A:419 forms conventional hydrogen bonds, while GLU A:401 and ASP A:418 participate in Pi-Anion interactions, potentially involving electrostatic stabilization. ALA A:349 forms a Pi-Alkyl interaction, further suggesting that hydrophobic and aromatic interactions are key to binding. The presence of Pi-Alkyl and alkyl interactions at VAL A:352 and ARG A:404 also highlights a significant role of hydrophobic forces in stabilizing the interaction. Additionally, PRO A:403 exhibits a carbon-hydrogen interaction, contributing to the overall binding. Overall, the variety of interaction types, including conventional hydrogen bonds, alkyl interactions, pi-stacking, and more specialized bonds like Pi-Anion and Pi-Sulfur, demonstrates the complexity of protein-ligand binding in the ZYMV-HC-Pro protein. These interactions suggest that licorice-derived compounds may effectively interact with the protein through a combination of hydrophobic, electrostatic, and aromatic interactions, providing valuable insights for further research into potential antiviral therapies. Data in Table (4 & Fig. 3) illustrates the bonding interactions between the amino acid residues in the ZYMV-P3 protein and four licorice-derived bioactive compounds: Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin. The interactions identified include a mixture of hydrophobic, hydrogen bonding, and aromatic interactions, each contributing to the stability and specificity of the protein-ligand binding. For Glycyrrhetic acid , the interaction profile shows a strong presence of hydrophobic interactions, notably with Alkyl bonds at ILE A:305 and HIS A:322. These alkyl interactions, especially when combined with the Pi-Alkyl bond at HIS A:304, indicate the importance of non-polar interactions in stabilizing the ligand-protein complex. The Pi-Sigma interaction at HIS A:322 further supports the aromatic stacking nature of the ligand's binding. Conventional hydrogen bonds at SER A:307 and the Carbon-Hydrogen interaction at HIS A:304 provide additional stabilization, ensuring a strong and diverse binding interface. With Isoliquiritin , several unfavorable interactions are noted, particularly the unfavorable donor-donor interactions at ARG A:327 and ASN A:325. These suggest that there may be some suboptimal binding in these regions, potentially due to steric clashes or electrostatic repulsion between the donor atoms. Despite these unfavorable interactions, Pi-Sigma interactions at ILE A:305 and Pi-Pi stacking at HIS A:322 highlight that aromatic interactions still play a key role in stabilizing the binding. The conventional hydrogen bond at ASP A:329 indicates a stabilizing interaction with polar residues, contributing to the overall binding. For Liquiritin , the interactions are largely similar to those seen with Isoliquiritin, with Pi-Pi stacking at HIS A:322 and Pi-Alkyl at ILE A:305 continuing to demonstrate the importance of aromatic and hydrophobic interactions. The conventional hydrogen bonds at SER A:307 and ARG A:327 further reinforce the stability of the complex, suggesting that both hydrophobic and polar interactions are contributing to the overall affinity of the ligand for the protein. Finally, Glabridin presents a more complex interaction profile. The Pi-Alkyl and Alkyl interactions at ARG A:327 and ILE A:305 suggest strong hydrophobic stabilizing forces, with multiple interactions at each site contributing to the overall binding. The Pi-Anion bond at ASP A:329 is another interesting feature, where electrostatic interactions likely enhance the stability of the binding at this site. Additionally, Pi-Pi stacking at HIS A:322 further supports the aromatic stabilization of the complex. The presence of unfavorable donor-donor interactions at ASN A:325, similar to what was observed with Isoliquiritin, again points to areas where ligand optimization could potentially improve the binding efficiency or reduce instability. Overall, the data reveals a mix of favorable and unfavorable interactions, with hydrophobic and aromatic interactions playing prominent roles in stabilizing the binding of the licorice-derived compounds to the ZYMV-P3 protein. The presence of unfavorable interactions in some cases suggests areas for potential optimization in the ligand structure. These insights into protein-ligand binding dynamics may contribute to the development of more effective antiviral strategies targeting ZYMV-P3. The results in Table 5 & Fig. 4 presented outlines the specific bonding interactions between four licorice-derived bioactive compounds—Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin—and the ZYMV-6K1 protein. These interactions help to identify how each compound binds to specific amino acid residues of the protein, which could provide insights into their potential biological activities or roles in therapeutic applications, particularly in relation to ZYMV (Zucchini yellow mosaic virus) infection. Glycyrrhetic acid forms a variety of bonding interactions with the ZYMV-6K1 protein. For example, the amino acid phenylalanine (PHE) at position A:23 forms an alkyl bond with Glycyrrhetic acid, indicating a hydrophobic interaction. Additionally, the interaction between IsoLeucine (ILE) at A:34 and Glycyrrhetic acid is more complex, involving alkyl, Pi-Alkyl, and conventional hydrogen bonds, suggesting a multifaceted mode of interaction that likely stabilizes the binding. Phenylalanine at A:32 also interacts via Pi-Alkyl bonding, highlighting its role in the aromatic π-π interactions that may contribute to the stability of the complex. Isoliquiritin interacts with ZYMV-6K1 through conventional hydrogen bonds with aspartic acid (ASP) at A:24 and arginine (ARG) at A:27, which are typical of electrostatic interactions. These hydrogen bonds can play a role in enhancing the binding specificity between the compound and the protein. The interaction of phenylalanine (PHE) at A:23 via Pi-Pi T-Shaped bonding indicates π-π stacking interactions, which are often seen in ligand-receptor binding where aromatic rings play a key role. IsoLeucine (ILE) at A:34 forms a Pi-Sigma bond with isoliquiritin, indicating another level of interaction between the compound and the protein's hydrophobic regions. Liquiritin also forms hydrogen bonds with ARG (A:27), similar to isoliquiritin, but it also exhibits an unfavorable donor-donor interaction with lysine (LYS) at A:37. This unfavorable interaction suggests that the binding of liquiritin might not be as stable in this region, potentially leading to a weaker or less specific binding at this site. As with the other compounds, phenylalanine (PHE) at A:23 forms a Pi-Pi T-Shaped interaction, contributing to a strong, stabilizing aromatic interaction. Additionally, ILE at A:34 forms Pi-Sigma interactions, further suggesting that the hydrophobic binding pocket of ZYMV-6K1 plays an essential role in binding liquiritin. Glabridin exhibits a complex pattern of bonding with ZYMV-6K1, with multiple interactions seen in the table. IsoLeucine (ILE) at A:34 forms a Pi-Sigma interaction, a common feature across several of the bioactive compounds, emphasizing the importance of hydrophobic interactions in these complexes. Valine (VAL) at A:41 engages in Pi-Alkyl bonding, reinforcing the importance of hydrophobic regions in stabilizing glabridin binding. Leucine (LEU) at A:38 forms Pi-Alkyl interactions, which could be involved in stabilizing the binding pocket. Interestingly, lysine (LYS) at A:37 is involved in multiple types of bonding, including Alkyl and Pi-Alkyl interactions, as well as a Pi-Cation bond. This suggests that lysine may play a critical role in facilitating strong, multifaceted binding with glabridin. Additionally, Leucine at A:16 forms multiple Pi-Alkyl and Alkyl interactions, contributing to the overall stability of the protein-ligand complex. In a conclusion, the interactions detailed in the table underscore the importance of both hydrophobic (alkyl, Pi-Alkyl) and electrostatic (hydrogen bonds) forces in mediating the binding of licorice-derived compounds to ZYMV-6K1. These interactions can provide insights into the structural dynamics of protein-ligand binding and may help guide the design of more effective bioactive molecules for therapeutic applications against ZYMV or other related viruses. The varied types of bonds also highlight the versatility of these compounds in recognizing and stabilizing interactions with different amino acid residues, which is critical for their potential efficacy. Results in Table 6 & Fig. 5 showed that the bonding interactions between four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-CI protein reveal a complex network of interactions that could help elucidate the binding dynamics of these compounds with the protein. Glycyrrhetic acid interacts with several amino acids in ZYMV-CI, exhibiting Pi-Alkyl interactions with Proline (PRO) at positions A:207 and A:378, which are indicative of hydrophobic bonding. These interactions suggest a strong hydrophobic interface that may contribute to the stability of the binding. Additionally, threonine (THR) at A:179 and serine (SER) at A:376 form carbon-hydrogen bonds with the compound, implying weaker, but still significant, electrostatic interactions. Proline at A:378 also forms multiple Pi-Alkyl bonds, further emphasizing the role of hydrophobic regions in stabilizing the complex. Histidine (HIS) at A:177 and threonine (THR) at A:205 participate in carbon-hydrogen and Pi-Donor-H bonds, respectively, suggesting that these residues play a supportive role in binding through weaker hydrogen bonds and donor interactions. Isoliquiritin, similar to Glycyrrhetic acid, interacts with threonine (THR) at A:205 through a Pi-Donor-H bond, which may facilitate the ligand's positioning within the protein’s binding pocket. Proline (PRO) at A:207 forms a Pi-Alkyl interaction, reinforcing hydrophobic binding. Isoliquiritin also establishes conventional hydrogen bonds with serine (SER) at A:376, and more importantly, it forms unfavorable donor-donor interactions with arginine (ARG) at A:209 and asparagine (ASN) at A:187. These unfavorable interactions may suggest less optimal binding or potential destabilization in certain regions. The conventional hydrogen bonds with ASN at A:187 further complicate the interaction profile, revealing possible competition or steric hindrance at this binding site. Liquiritin shares several interactions with isoliquiritin, including Pi-Alkyl interactions with Proline (PRO) at A:207 and Pi-Donor-H interactions with threonine (THR) at A:205. Glycine (GLY) at A:208 forms both conventional hydrogen bonds and Pi-Donor-H bonds with the compound, which may help anchor the compound within the protein. However, like isoliquiritin, liquiritin also exhibits unfavorable donor-donor interactions with asparagine (ASN) at A:310 and A:187. These unfavorable interactions again suggest potential instability or weak binding at these sites, possibly reducing the overall binding affinity in these regions. Glabridin’s interactions with ZYMV-CI are marked by several key features. Proline (PRO) at A:207 forms alkyl bonds, which are likely to contribute to hydrophobic interactions. Similar to other compounds, glabridin interacts with threonine (THR) at A:179 and serine (SER) at A:376 through Pi-Donor-H bonds, indicating a preference for donor-acceptor interactions in these regions. Proline at A:378 also forms multiple Pi-Alkyl bonds, as well as a Pi-Sigma bond, suggesting a particularly strong hydrophobic interaction at this site. The compound's interactions with Histidine (HIS) at A:177 and threonine (THR) at A:205 through carbon-hydrogen and Pi-Donor-H bonds demonstrate the importance of both hydrogen and donor interactions in the overall binding of glabridin. In summary, the interactions between the licorice-derived bioactive compounds and ZYMV-CI indicate a mixture of hydrophobic, hydrogen bonding, and donor-acceptor interactions. The hydrophobic interactions, especially with Proline and threonine, seem to play a major role in stabilizing the compounds within the protein. At the same time, the presence of unfavorable donor-donor interactions in some cases suggests that the binding may not be perfectly optimized, potentially reducing the affinity or stability of the ligand-protein complex at certain sites. These findings provide insights into how these compounds may interact with ZYMV-CI and could be useful for designing more effective therapeutics targeting this protein. Results in Table 7 & Fig. 6 detailing the bonding interactions between four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-6K2 protein provides valuable insights into the nature of these interactions, which could influence the binding affinity and stability of the protein-ligand complexes. Glycyrrhetic acid interacts primarily with tryptophan (TRP) at position D:36 through multiple Pi-Alkyl bonds. These interactions, characteristic of hydrophobic regions, suggest that tryptophan’s aromatic ring plays a significant role in stabilizing the binding of Glycyrrhetic acid. The multiple Pi-Alkyl interactions likely contribute to the overall strength and specificity of this binding site, with tryptophan acting as a key residue in the protein-ligand interaction. Isoliquiritin binds with ZYMV-6K2 through a variety of interactions. Asparagine (ASN) at D:22 forms conventional hydrogen bonds with the compound, while also displaying an unfavorable donor-donor interaction, which could reduce the overall binding efficiency or stability at this site. The interaction of tryptophan (TRP) at D:15 with isoliquiritin involves Pi-Pi stacked bonding, which is indicative of aromatic stacking interactions that contribute to the stability of the complex. Lysine (LYS) at D:19 participates in Pi-Alkyl interactions, highlighting its role in stabilizing the hydrophobic portion of the ligand. Aspartic acid (ASP) at D:23 interacts through Pi-Anion bonding, as well as conventional hydrogen bonds, and also displays an unfavorable donor-donor interaction, suggesting potential areas of weaker or less optimal binding. Liquiritin engages with ZYMV-6K2 through van der Waals forces with glycine (GLY) at D:33, which are typically weak but can help to fine-tune the overall binding interaction. Methionine (MET) at D:29 forms Pi-Alkyl interactions, contributing to the hydrophobic stabilization of the ligand in the binding pocket. Additionally, Leucine (LEU) at D:32 forms amide-Pi stacked interactions, which suggest that the compound may benefit from multiple levels of stabilization through both hydrophobic and potential hydrogen bonding interactions, further enhancing the overall stability of the complex. Glabridin interacts with ZYMV-6K2 through several key residues. Lysine (LYS) at D:19 forms both Pi-Alkyl and alkyl bonds with the compound, indicating that its hydrophobic side chains contribute to stabilizing the binding site. Tryptophan (TRP) at D:15 shows an even more intricate pattern of interactions, with Pi-Alkyl, alkyl, and Pi-Pi stacked bonds. These multiple interactions, particularly the Pi-Pi stacking, suggest that tryptophan plays a central role in the binding of glabridin, likely stabilizing the complex through aromatic interactions. In summary, the bonding interactions between the licorice-derived compounds and ZYMV-6K2 highlight a combination of hydrophobic (Pi-Alkyl, Pi-Pi stacked), electrostatic (conventional hydrogen bonds, Pi-Anion), and weak van der Waals interactions. These interactions indicate that hydrophobic regions, particularly involving tryptophan, lysine, and methionine, play a critical role in stabilizing the binding of the compounds to the protein. However, the presence of unfavorable donor-donor interactions in some cases, such as with asparagine and aspartic acid, may suggest areas where the binding is less stable or efficient, potentially limiting the overall effectiveness of these compounds in modulating ZYMV-6K2 activity. Results in Table 8 & Fig. 7 demonstrated that the interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-NIa-VPg protein provide a detailed look at how these compounds bind to various amino acid residues, potentially influencing the protein's function and stability. Glycyrrhetic acid binds with several amino acids in ZYMV-NIa-VPg, primarily through hydrophobic interactions. Proline (PRO) at position A:143 forms carbon-hydrogen and alkyl bonds, indicating that the compound interacts with the hydrophobic regions of the protein. Similarly, Valine (VAL) at A:96 and IsoLeucine (ILE) at A:93 form alkyl interactions, which help anchor the compound within the protein's binding pocket. IsoLeucine at A:124 and Leucine (LEU) at A:141 also contribute to the binding with alkyl interactions, further stabilizing the compound through hydrophobic forces. These interactions suggest that the binding of Glycyrrhetic acid to ZYMV-NIa-VPg is largely driven by hydrophobic interactions, which are critical for stabilizing the ligand within the protein. Isoliquiritin interacts with ZYMV-NIa-VPg through a variety of bonding mechanisms. Aspartic acid (ASP) at A:78 forms conventional hydrogen bonds with isoliquiritin, enhancing its stability in the binding pocket. Threonine (THR) at A:91, however, exhibits an unfavorable acceptor-acceptor interaction, suggesting that this particular binding site might not be optimal for isoliquiritin, possibly reducing its overall binding affinity. Threonine at A:89 forms conventional hydrogen bonds, further stabilizing the interaction. IsoLeucine (ILE) at A:124 interacts via Pi-Sigma and Pi-Alkyl bonding, indicating the presence of both aromatic and hydrophobic interactions that contribute to the overall binding strength. Liquiritin binds to ZYMV-NIa-VPg through several hydrophobic interactions, as well as hydrogen bonding. Lysine (LYS) at A:121 forms conventional hydrogen bonds, suggesting some electrostatic contribution to the binding. Aspartic acid (ASP) at A:78 also forms conventional hydrogen bonds, further contributing to the stabilization of the ligand-protein complex. Leucine (LEU) at A:141 forms Pi-Sigma interactions, likely stabilizing the complex through aromatic interactions. IsoLeucine (ILE) at A:124 participates in Pi-Sigma bonding, contributing to the overall stability of the interaction. Additionally, Valine (VAL) at A:96 and IsoLeucine (ILE) at A:93 form Pi-Alkyl bonds, which further stabilize the binding through hydrophobic interactions, suggesting that the ligand binds primarily through non-polar forces. Glabridin shows a similar interaction profile to the other compounds, with multiple hydrophobic interactions that contribute to the binding stability. Leucine (LEU) at A:141 forms Pi-Alkyl bonds, stabilizing the complex through hydrophobic interactions. IsoLeucine (ILE) at A:124 engages in a complex set of interactions, including alkyl, Pi-Alkyl, Pi-Alkyl, and Pi-Sigma bonds. These multiple types of bonding suggest that IsoLeucine at this site plays a critical role in stabilizing glabridin binding through a combination of hydrophobic and aromatic interactions. IsoLeucine at A:93 also forms alkyl, Pi-Alkyl, and Pi-Sigma bonds, further reinforcing the binding of glabridin to the protein. Finally, Valine (VAL) at A:96 contributes to the binding through Pi-Alkyl interactions, stabilizing the hydrophobic regions of the protein-ligand complex. In summary, the bonding interactions between these licorice-derived compounds and the ZYMV-NIa-VPg protein are dominated by hydrophobic interactions, particularly those involving alkyl, Pi-Alkyl, and Pi-Sigma bonds. These interactions are critical for stabilizing the binding of the compounds within the protein's hydrophobic pockets. Additionally, the presence of conventional hydrogen bonds, as seen with aspartic acid and lysine, suggests that electrostatic interactions also play a role in stabilizing the complexes. The unfavorable acceptor-acceptor interactions observed with isoliquiritin indicate that not all binding sites are equally favorable for these compounds, which may affect the overall binding affinity and specificity. These findings suggest that the ligands interact primarily through non-polar forces, with some contributions from hydrogen bonding, making the protein-ligand interactions potentially more dynamic and adaptable for therapeutic targeting. The bonding interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-NIa-Pro protein (Table 9 & Fig. 8) demonstrate a range of hydrophobic and electrostatic interactions that likely influence the binding efficiency and stability of the complexes. Glycyrrhetic acid interacts with several key amino acids in ZYMV-NIa-Pro, with a primary focus on hydrophobic interactions. Lysine (LYS) at A:6 and tyrosine (TYR) at A:11 form conventional hydrogen bonds, indicating that these residues contribute to the electrostatic stabilization of the compound within the protein. Valine (VAL) at A:125 interacts through alkyl bonds, which stabilize the ligand through hydrophobic interactions. Tyrosine at A:5 contributes to the binding with a Pi-Alkyl interaction, suggesting that the aromatic ring of tyrosine is involved in stabilizing the interaction through π-π interactions. These hydrophobic interactions, along with conventional hydrogen bonds, suggest that Glycyrrhetic acid binds primarily through both electrostatic and hydrophobic forces. Isoliquiritin binds with ZYMV-NIa-Pro through a combination of conventional hydrogen bonds and aromatic interactions. Alanine (ALA) at A:170 forms Pi-Sigma and conventional hydrogen bonds with the compound, stabilizing the interaction through both electrostatic and π-π interactions. Glycine (GLY) at A:168 also forms conventional hydrogen bonds, further contributing to the stabilization of the complex. However, lysine (LYS) at A:29 exhibits an unfavorable acceptor-acceptor interaction, indicating that this particular region may not be optimal for binding, potentially reducing the stability of the complex at this site. Threonine (THR) at A:146 contributes to the binding through conventional hydrogen bonds, supporting the overall stability of the ligand within the protein. Liquiritin exhibits multiple interactions with ZYMV-NIa-Pro, including both hydrophobic and electrostatic bonding. Glutamic acid (GLU) at A:220 and A:30 forms unfavorable acceptor-acceptor interactions and conventional hydrogen bonds, respectively. The unfavorable interaction at A:220 suggests a less favorable binding region, while the conventional hydrogen bond at A:30 helps stabilize the binding. Alanine (ALA) at A:170 forms Pi-Alkyl interactions, contributing to the hydrophobic stabilization of the ligand. Cysteine (CYS) at A:151 forms Pi-Alkyl bonds, further stabilizing the complex through hydrophobic interactions. Asparagine (ASN) at A:147 and threonine (THR) at A:146 contribute conventional hydrogen bonds, further enhancing the overall binding affinity. Glutamine (GLN) at A:221 also forms a conventional hydrogen bond, supporting the electrostatic stabilization of the ligand. Glabridin interacts with ZYMV-NIa-Pro through specific hydrophobic and electrostatic interactions. Glutamic acid (GLU) at A:148 forms Pi-Anion bonds with the compound, stabilizing the interaction through electrostatic forces. Alanine (ALA) at A:170 forms Pi-Alkyl bonds, contributing to the hydrophobic interaction. These interactions suggest that Glabridin binds primarily through hydrophobic and electrostatic forces, with glutamic acid and alanine playing key roles in stabilizing the complex. In summary, the bonding interactions of the licorice-derived compounds with ZYMV-NIa-Pro are characterized by a mix of hydrophobic interactions (such as alkyl, Pi-Alkyl, and Pi-Sigma) and electrostatic interactions (including conventional hydrogen and Pi-Anion bonds). These interactions collectively contribute to the stability and specificity of the complexes. However, the presence of unfavorable donor-acceptor interactions, such as those with lysine in Isoliquiritin and glutamic acid in Liquiritin, suggests that some regions of the binding sites are less optimal for certain compounds, which may reduce the overall binding strength or efficiency. Nonetheless, these findings provide important insights into the potential for these bioactive compounds to modulate the activity of ZYMV-NIa-Pro. The bonding interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-NIb protein (Table 10 & Fig. 9) reveal a complex set of interactions, highlighting both hydrophobic and electrostatic forces, which likely contribute to the stability and specificity of the binding. Glycyrrhetic acid shows strong hydrophobic interactions with several amino acids in ZYMV-NIb, primarily through alkyl and Pi-Alkyl interactions. Leucine (LEU) at positions A:122, A:152, and A:198, along with Valine (VAL) at A:202 and methionine (MET) at A:281, contribute alkyl bonds, stabilizing the compound through hydrophobic interactions. Tyrosine (TYR) at A:119 interacts via Pi-Sigma bonding, further reinforcing the stability of the complex through aromatic interactions. Phenylalanine (PHE) at A:140 also participates in Pi-Alkyl bonds, highlighting the importance of aromatic and hydrophobic interactions in stabilizing Glycyrrhetic acid within the binding pocket. However, arginine (ARG) at A:148 forms an unfavorable donor-donor interaction, indicating that this site might not contribute optimally to the binding, potentially destabilizing the interaction at this location. Serine (SER) at A:121 and cysteine (CYS) at A:203 form conventional hydrogen bonds, further contributing to the stabilization of Glycyrrhetic acid in the protein's binding site. Lysine (LYS) at A:135 also participates in a conventional hydrogen bond, adding to the overall electrostatic stabilization of the complex. Isoliquiritin interacts with ZYMV-NIb through a combination of Pi-Sigma, conventional hydrogen, and hydrophobic bonds. Threonine (THR) at A:81 forms Pi-Sigma bonds with the compound, stabilizing the interaction through aromatic interaction. Asparagine (ASN) at A:184 contributes conventional hydrogen bonds, as does aspartic acid (ASP) at A:253 and A:352, providing additional electrostatic stabilization. However, the serine (SER) at A:254 forms an unfavorable donor-donor interaction, which may reduce the stability of the binding at this site. Arginine (ARG) at A:187 forms Pi-Alkyl and conventional hydrogen bonds, contributing both hydrophobic and electrostatic forces to the binding, while lysine (LYS) at A:185 stabilizes the complex through Pi-Alkyl interactions. Liquiritin shows a broad range of interactions, with both hydrophobic and electrostatic components. Glutamic acid (GLU) at A:116 and IsoLeucine (ILE) at A:118 form carbon-hydrogen bonds, contributing weaker interactions that may help position the compound in the binding pocket. Serine (SER) at A:121 forms conventional hydrogen bonds, stabilizing the binding. Leucine (LEU) at A:198 participates in Pi-Sigma bonding, enhancing the hydrophobic stabilization of the complex. Tyrosine (TYR) at A:119 forms a Pi-Pi T-shaped interaction, indicative of aromatic stacking, which likely helps in stabilizing the ligand. Valine (VAL) at A:202 forms Pi-Alkyl bonds, further stabilizing the interaction through hydrophobic forces. Aspartic acid (ASP) at A:205 and A:206 contribute conventional hydrogen bonds, while phenylalanine (PHE) at A:207 participates in both conventional hydrogen bonding and carbon-hydrogen bonding, offering both electrostatic and hydrophobic stabilization to the complex. Glabridin interacts with ZYMV-NIb primarily through alkyl and conventional hydrogen bonds. Serine (SER) at A:310 forms a conventional hydrogen bond, helping to stabilize the ligand within the binding pocket. Arginine (ARG) at A:187 and lysine (LYS) at A:185 form alkyl bonds, contributing hydrophobic stabilization, while lysine at A:304 forms a conventional hydrogen bond, further stabilizing the binding. The presence of alkyl interactions in key positions suggests that the binding of Glabridin is largely driven by hydrophobic forces, with some additional electrostatic contributions from the hydrogen bonds. In summary, the interactions between the licorice-derived bioactive compounds and ZYMV-NIb are dominated by hydrophobic interactions, particularly those involving alkyl, Pi-Alkyl, Pi-Sigma, and Pi-Pi bonds. These interactions suggest that the compounds primarily interact with hydrophobic regions of the protein, stabilizing the complexes within the binding site. Additionally, conventional hydrogen bonds and some unfavorable donor-donor interactions contribute to the overall binding stability. The presence of unfavorable interactions, such as those with serine in Isoliquiritin and glutamic acid in Liquiritin, may indicate regions of suboptimal binding, which could reduce the overall binding efficiency of the complexes. Nonetheless, these findings highlight the significant role of hydrophobic interactions in the binding of licorice-derived compounds to ZYMV-NIb, suggesting that these compounds may serve as potential modulators of protein function through their binding dynamics. The bonding interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-CP protein (Table 11 & Fig. 10) reflect a range of interactions, with hydrophobic forces and electrostatic bonds playing significant roles in stabilizing the binding of these compounds to the protein. Glycyrrhetic acid primarily forms hydrophobic interactions with several amino acids in ZYMV-CP, with alkyl and Pi-Alkyl interactions at key positions. Alanine (ALA) at B:39 engages in both alkyl and Pi-Alkyl bonds, which help anchor the compound within the protein’s hydrophobic pocket. Lysine (LYS) at C:44 forms conventional hydrogen bonds, contributing to the electrostatic stabilization of the complex. Phenylalanine (PHE) at C:36 and lysine (LYS) at C:34 contribute alkyl interactions, further stabilizing the binding through hydrophobic forces. These interactions suggest that Glycyrrhetic acid binds primarily through hydrophobic forces, with some additional electrostatic stabilization provided by conventional hydrogen bonds. Isoliquiritin interacts with ZYMV-CP through a combination of hydrophobic and electrostatic bonds. Lysine (LYS) at C:41 forms Pi-Alkyl bonds, indicating the presence of both hydrophobic and π-π interactions that contribute to stabilizing the ligand in the protein's binding pocket. Proline (PRO) at C:38 forms conventional hydrogen bonds, adding to the electrostatic stabilization. However, arginine (ARG) at C:42 forms an unfavorable donor-donor interaction, which could reduce the overall binding strength at this site. Lysine (LYS) at C:44 forms a more favorable combination of Pi-Alkyl, conventional hydrogen, and Pi-Anion interactions, contributing significantly to the stability of the complex. Aspartic acid (ASP) at C:30 forms a Pi-Cation interaction, suggesting that electrostatic interactions also play a role in stabilizing the binding. Additionally, Leucine (LEU) at C:29 engages in Pi-Sigma bonding, which further strengthens the hydrophobic component of the binding. Liquiritin shows a variety of bonding types with ZYMV-CP, including both hydrophobic and electrostatic interactions. Arginine (ARG) at C:23 forms unfavorable donor-donor interactions along with conventional hydrogen bonds, indicating that the binding at this site may not be ideal. Asparagine (ASN) at B:37 and phenylalanine (PHE) at C:31 both form conventional hydrogen bonds, helping stabilize the ligand in the protein. Alanine (ALA) at B:39 forms Pi-Alkyl bonds, contributing to the hydrophobic stabilization of the complex. Arginine (ARG) at B:42 forms a conventional hydrogen bond, further supporting the electrostatic stabilization of the binding. Glutamic acid (GLU) at C:26 forms multiple conventional hydrogen bonds and carbon-hydrogen interactions, contributing to both electrostatic and hydrophobic stabilization of the ligand. Glabridin interacts with ZYMV-CP through a combination of hydrophobic and electrostatic forces. Alanine (ALA) at A:39 forms both Pi-Sigma and alkyl bonds, suggesting that this site is crucial for stabilizing the compound through both hydrophobic and aromatic interactions. Aspartic acid (ASP) at B:30 forms conventional hydrogen and Pi-Cation bonds, which stabilize the complex through electrostatic interactions. Arginine (ARG) at A:42 forms a Pi-Anion bond, indicating a significant contribution of electrostatic forces to the binding. Alanine (ALA) at B:27 forms Pi-Alkyl bonds, further contributing to the hydrophobic stabilization of the ligand. Proline (PRO) at A:38 also forms Pi-Alkyl bonds, supporting the hydrophobic nature of the binding. In summary, the bonding interactions between the licorice-derived bioactive compounds and ZYMV-CP are characterized by a blend of hydrophobic and electrostatic forces. The majority of interactions involve alkyl, Pi-Alkyl, Pi-Sigma, and Pi-Anion bonds, highlighting the importance of hydrophobic interactions in stabilizing these complexes. Conventional hydrogen bonds contribute further to the electrostatic stabilization of the protein-ligand interactions. However, the presence of unfavorable donor-donor interactions, as seen with arginine in Isoliquiritin and Liquiritin, and glutamic acid in Liquiritin, suggests that some regions of the binding sites may not be optimal for these compounds, potentially reducing their overall binding affinity. Despite this, the predominance of hydrophobic interactions suggests that these compounds primarily stabilize their binding to ZYMV-CP through non-polar interactions, which could be critical for modulating the protein's function or activity. Discussion Regarding ZTMV-P1 protein the data highlighted various bonding interactions between licorice-derived bioactive compounds and the ZYMV-P1 protein, including hydrogen bonds, alkyl interactions, Pi-Alkyl, and Pi-based interactions. These interactions play a crucial role in stabilizing the protein-ligand complex, particularly hydrogen bonds, which contribute significantly to the binding affinity and specificity of the compounds. This is consistent with previous studies indicating the importance of hydrogen bonding in protein-ligand recognition and stability [22, 23]. Hydrophobic interactions, including alkyl and Pi-Alkyl interactions, also contribute to stabilizing the binding of non-polar ligands. These interactions are critical for the binding of larger ligands and enhance stability through aromatic stacking [24]. The prevalence of these interactions suggests that licorice compounds likely use hydrophobic and aromatic forces to interact with the ZYMV-P1 protein, contributing to their antiviral potential. The analysis also identifies unfavorable donor-donor and acceptor-acceptor interactions, which are energetically less favorable and can cause steric clashes. These interactions highlight areas for ligand optimization, as modifying functional groups to avoid such clashes could enhance binding affinity and specificity [25]. Addressing these unfavorable interactions could improve the potency of these compounds as antiviral agents [26]. These findings suggest that licorice-derived compounds like glycyrrhizin could serve as a promising foundation for antiviral drug development. By optimizing their interactions with viral proteins and reducing unfavorable interactions, researchers can design more effective inhibitors targeting ZYMV and related viruses. Natural compounds like those derived from licorice offer a potential alternative to synthetic drugs, providing safer and more targeted antiviral therapies [27]. The interactions between the ZYMV-HC-Pro protein and four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-demonstrate a complex range of bonding types, including conventional hydrogen bonds, hydrophobic alkyl interactions, pi-stacking interactions, and specialized Pi-Anion and Pi-Sulfur bonds. These findings indicate the multifaceted nature of protein-ligand binding and the potential of these compounds as inhibitors of ZYMV-HC-Pro. Glycyrrhetic Acid interactions are primarily dominated by hydrophobic alkyl bonds with residues like CYS A:342 and ALA A:337. Hydrogen bonds at TYR A:335 further stabilize the binding, suggesting a highly favorable binding environment [28]. Isoliquiritin shows significant aromatic interactions, including Pi-Alkyl interactions at VAL A:352 and Pi-Anion interactions at GLU A:401, which contribute to its binding stability [24]. The diversity of bonding types at GLU A:401 indicates a complex and specific binding mode. Liquiritin engages in both hydrogen bonding and Pi-Sulfur interactions, the latter being important for enzyme-inhibitor complexes [29]. However, an unfavorable donor-donor interaction at HIS A:415 suggests opportunities for ligand optimization [26]. Glabridin interacts through a combination of conventional hydrogen bonds and specialized Pi-Anion bonds at GLU A:401 and ASP A:418, along with hydrophobic interactions like Pi-Alkyl at ALA A:349. These interactions indicate a strong binding affinity driven by both electrostatic and hydrophobic forces [28]. The interactions between the ZYMV-P3 protein and four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-reveal a range of hydrophobic, aromatic, and polar interactions, all contributing to binding stability and specificity. Glycyrrhetic Acid demonstrates hydrophobic alkyl bonds at ILE A:305 and HIS A:322, which stabilize the ligand within a non-polar binding pocket. Pi-Alkyl and Pi-Sigma interactions further reinforce the binding, while conventional hydrogen bonds at SER A:307 enhance the overall affinity [28, 24]. This combination of interactions suggests a stable, energetically favorable complex. Isoliquiritin exhibits some unfavorable donor-donor interactions at ARG A:327 and ASN A:325, indicating areas for optimization [26]. However, it also maintains stabilizing Pi-Sigma and Pi-Pi stacking interactions at ILE A:305 and HIS A:322, contributing to overall binding stability. A conventional hydrogen bond at ASP A:329 also enhances the interaction. Liquiritin shares similar interactions with Isoliquiritin, with key Pi-Pi stacking and Pi-Alkyl interactions at HIS A:322 and ILE A:305. Conventional hydrogen bonds further stabilize the binding, although unfavorable donor-donor interactions at ASN A:325 suggest optimization opportunities. Glabridin has a more complex interaction profile, with strong hydrophobic and Pi-Anion interactions at ARG A:327, ILE A:305, and ASP A:329, contributing to overall stability. Pi-Pi stacking interactions at HIS A:322 also play a role. However, it shares the unfavorable donor-donor interactions seen in Isoliquiritin, indicating areas for improvement in the ligand structure. The analysis of the bonding interactions between licorice-derived bioactive compounds and the ZYMV-CI protein reveals the importance of hydrophobic, electrostatic, and donor-acceptor interactions in stabilizing the ligand-protein complex. Glycyrrhetic acid shows strong Pi-Alkyl interactions, particularly with Proline residues, and weaker electrostatic contributions, suggesting a balanced binding profile [24]. Isoliquiritin and Liquiritin share similar profiles but exhibit unfavorable donor-donor interactions with asparagine and arginine, potentially destabilizing the complex in these regions [26]. These steric clashes or electrostatic repulsions highlight areas for optimization to improve binding affinity. Glabridin, like the other compounds, demonstrates hydrophobic interactions (Pi-Alkyl) with Proline and additional donor-acceptor bonds, further stabilizing the complex [26]. These interactions collectively emphasize the crucial role of hydrophobic regions, especially the Pi-Alkyl bonds, in stabilizing the complexes, while electrostatic interactions help enhance specificity and binding strength. The analysis of bonding interactions between licorice-derived bioactive compounds and the ZYMV-6K2 protein reveals key insights into the stability and specificity of the protein-ligand complex. Glycyrrhetic acid forms strong Pi-Alkyl interactions with tryptophan (TRP) residues, which play a pivotal role in stabilizing the binding, underlining the importance of hydrophobic interactions in protein-ligand binding [24]. Isoliquiritin shares similar hydrophobic interactions but also exhibits unfavorable donor-donor interactions with asparagine (ASN), suggesting areas for improvement in binding efficiency [26]. Additionally, it demonstrates aromatic interactions with TRP and hydrophobic contributions from lysine (LYS) residues, which enhance the stability of the complex [24]. Liquiritin also interacts with hydrophobic residues like methionine (MET) and Leucine (LEU) through Pi-Alkyl and amide-Pi stacking interactions. However, it similarly presents unfavorable donor-donor interactions with ASN residues, which could reduce binding stability [26]. Glabridin, like the other compounds, benefits from hydrophobic interactions with TRP and LYS residues, with Pi-Pi stacking providing additional stability. However, unfavorable donor-donor interactions with ASN residues highlight areas for optimization [24]. The bonding interactions between the four licorice-derived bioactive compounds and the ZYMV-NIa-VPg protein reveal that hydrophobic interactions are the primary stabilizing force, with hydrogen bonding also contributing to the overall binding stability. Glycyrrhetic acid primarily forms hydrophobic interactions, particularly with Proline (PRO), Valine (VAL), and IsoLeucine (ILE), highlighting the importance of non-polar forces in stabilizing the complex [28]. These hydrophobic interactions suggest the ligand fits well into the protein's hydrophobic pocket, reinforcing its stability [24]. Isoliquiritin engages in both hydrophobic and electrostatic interactions, with hydrogen bonds formed with aspartic acid (ASP) and threonine (THR). However, unfavorable acceptor-acceptor interactions at THR suggest areas where optimization could improve binding efficiency [26]. The presence of both aromatic and hydrophobic interactions indicates a combination of forces that stabilize the ligand-protein complex [28]. Liquiritin’s binding is similarly dominated by hydrophobic interactions, particularly with residues like Leucine (LEU), IsoLeucine (ILE), and Valine (VAL), which form Pi-Sigma, Pi-Alkyl, and alkyl bonds. Additionally, hydrogen bonds with aspartic acid (ASP) and lysine (LYS) further stabilize the complex [24]. These interactions emphasize the role of hydrophobic forces in stabilizing the complex [24]. Glabridin also shows a similar profile, with hydrophobic interactions formed with IsoLeucine (ILE) and Leucine (LEU). These interactions, along with multiple types of bonds, suggest that hydrophobic forces dominate the binding process, contributing to the overall stability of the complex [28]. The results highlight the critical role of hydrophobic interactions, particularly alkyl, Pi-Alkyl, and Pi-Sigma bonds, in stabilizing these licorice-derived compounds within the ZYMV-NIa-VPg binding pocket. While electrostatic interactions also contribute, the presence of unfavorable interactions, especially with certain residues like threonine, suggests areas where ligand optimization could improve binding affinity and stability [26]. These findings offer valuable insights into developing more effective therapeutic agents targeting ZYMV. The interactions between the four licorice-derived bioactive compounds and the ZYMV-NIa-Pro protein involve both hydrophobic and electrostatic forces, affecting binding stability and specificity. Glycyrrhetic Acid Primarily forms hydrophobic (alkyl, Pi-Alkyl) interactions with Valine and Tyrosine, alongside electrostatic hydrogen bonds with Lysine and Tyrosine, stabilizing the complex [28]. Isoliquiritin, forms both hydrogen bonds and aromatic interactions. However, the Lysine residue creates an unfavorable interaction, which may decrease binding stability [26]. Liquiritin engages in hydrophobic (Pi-Alkyl) and electrostatic interactions, though unfavorable acceptor-acceptor interactions at certain sites reduce binding efficiency [24]. Glabridin binds through hydrophobic interactions (Pi-Alkyl) and electrostatic Pi-Anion bonds with Glutamic acid, contributing to stability [26]. The interactions between licorice compounds with ZYMV-NIb involve a mix of hydrophobic and electrostatic forces that stabilize the protein-ligand complexes and influence binding specificity. Glycyrrhetic acid forms strong hydrophobic interactions (alkyl, Pi-Alkyl) with residues like Leucine, Valine, and Methionine, alongside electrostatic stabilization via hydrogen bonds with Serine and Lysine. However, an unfavorable donor-donor interaction with Arginine may weaken binding at this site [28]. Isoliquiritin shows hydrophobic (Pi-Sigma, Pi-Alkyl) and electrostatic (hydrogen) interactions. However, the donor-donor interaction with Serine at A:254 reduces stability at this site [26], although other interactions stabilize the complex, such as Pi-Alkyl with Lysine and Arginine [24]. Liquiritin forms hydrophobic (Pi-Alkyl, Pi-Sigma) and electrostatic interactions with residues like Leucine, Tyrosine, and Aspartic acid. However, weak interactions at some sites, like Glutamic acid, may limit binding efficiency [28]. Glabridin primarily forms hydrophobic alkyl interactions with Arginine and Lysine, alongside hydrogen bonds, to stabilize the complex [24]. The interactions between these compounds with ZYMV-CP involve a combination of hydrophobic and electrostatic forces that contribute to the stability and specificity of the protein-ligand complexes. Glycyrrhetic acid primarily forms hydrophobic interactions (alkyl, Pi-Alkyl) with residues like Alanine, Phenylalanine, and Lysine, anchoring it within the protein's hydrophobic pocket. Additionally, Lysine forms hydrogen bonds, contributing to electrostatic stabilization [28]. Isoliquiritin interacts via Pi-Alkyl bonds with Lysine, while hydrogen bonds with Proline and favorable interactions with Lysine and Aspartic acid further stabilize the complex. However, an unfavorable donor-donor interaction with Arginine weakens binding at this site [24, 26]. Liquiritin forms a combination of hydrophobic and electrostatic interactions, such as Pi-Alkyl bonds with Alanine and hydrogen bonds with Asparagine and Phenylalanine. The presence of unfavorable donor-donor interactions with Arginine suggests certain regions may be suboptimal for binding [28]. Glabridin binds through hydrophobic interactions (Pi-Sigma, alkyl) with Alanine, along with hydrogen and Pi-Cation bonds from Aspartic acid, and Pi-Anion interactions with Arginine. These forces stabilize the ligand primarily through non-polar interactions [24]. In a conclusion, hydrophobic interactions, particularly alkyl, Pi-Alkyl, and Pi-Sigma bonds, dominate the binding of these compounds to ZYMV-CP. Electrostatic hydrogen bonds also contribute to stability, though unfavorable donor-donor interactions in some regions may weaken the binding. Conclusion Licorice-derived bioactive compounds demonstrate strong potential as antiviral agents due to their ability to form stable protein-ligand complexes with ZYMV proteins. Hydrophobic interactions, such as alkyl and Pi-based bonds, play a central role in stabilizing these complexes, while electrostatic hydrogen bonds further enhance binding affinity and specificity. Though some unfavorable interactions suggest opportunities for optimization, modifying these compounds can improve their antiviral potential. Overall, these natural compounds offer a promising alternative to synthetic drugs and could serve as the basis for more targeted, effective therapies against ZYMV and related viruses. Abbreviations ZYMV; Zucchini yellow mosaic virus, PDB; Protein Data Bank, 2D; Two D structure, 3D; Three D structures, GLY; Glycine, THR; Threonine, VAL; Valine, LYS; Lysine, GLU; Glutamic acid, ARG; Arginine, TYR; Tyrosine, GLN; Glutamine, PHE; Phenylalanine, SER; Serine, HIS; Histidine, LEU ; Leucine, ASP; Aspartic acid, ASN; Asparagine, CYS; Cysteine, ILE; IsoLeucine, ALA; Alanine, PRO; Proline, TRP; Tryptophan, and MET; Methionine. Declarations Ethics approval and consent to participate This study involved only plant and microbial samples, which do not require ethical approval under current research guidelines for human or animal subjects. Consent for Publication Not applicable. This study does not involve any personal data or information requiring consent for publication. Availability of data and material s No new datasets were generated or analyzed during the course of this study. Competing Interests The authors declare no competing interests. There are no financial, personal, or professional relationships that could have influenced the outcomes of this study. Funding The authors declare that no funding, grants, or other financial support was received for the preparation of this manuscript. Authors’ contributions Shrouk E.E. Farag conceptualized the study, gathered molecular nucleotide data, performed genetic variability analysis of ZYMV, and drafted the initial manuscript. Shafik D. Ibrahim carried out the protein-level analyses, evaluated genetic diversity using protein sequences, interpreted findings, and participated in manuscript revision. Atef S. Sadik oversaw the research process, ensured methodological rigor, contributed to the study design, and was actively involved in reviewing and approving the final manuscript. Mamdouh H. Abdel-Gaffar provided expertise in bioinformatics and phylogenetic analysis, supported the comparative genomics component, and contributed to the study design and manuscript development. Acknowledgments The authors extend their sincere gratitude to Miss El-Shymaa Tarek for her valuable assistance with the molecular docking analysis. Her guidance and support throughout the research process were greatly appreciated. Clinical Trial Number Not applicable References Ahsan M, Ashfaq M, Amer MA, Shakeel MT, Mehmood MA, Umar M, et al. Zucchini yellow mosaic virus (ZYMV) as a serious biotic stress to cucurbits: prevalence, diversity, and its implications for crop sustainability. Plants, 2023;12(19):3503. ‏ https://doi.org/10.3390/plants12193503 Al-Tamimi N, Kawas H, Mansour A, Salem N. Biological and molecular characterization of some Zucchini yellow mosaic virus isolates from Southern Syria and Jordan valley. Jordan Journal of Agricultural Sciences, 2010;6(3):1-15. ‏ Kamal R, Gusain YS, Kumar V, Sharma AK. Disease management through biological control agents: An eco-friendly and cost effective approach for sustainable agriculture-A Review. Agricultural Reviews, 2015; 36 (1):37-45. ‏ Velasco L, Ruiz L, Galipienso L, Rubio L, Janssen D. A historical account of viruses in intensive horticultural crops in the Spanish Mediterranean Arc: New challenges for a sustainable agriculture. Agronomy, 2020;10(6):1-26. Srivastava RM, Joshih S. Integrated pest management for cucurbits in cucumber ( Cucumis sativus L.). Cucumber Economic Values and Its Cultivation and Breeding, 2021;1(5):1-10. ‏ Baldodiya GM, Saikia R, Paswan RR, Borah BK. Sustainable agriculture and viral diseases of plants: An overview. New and Future Developments in Microbial Biotechnology and Bioengineering, 2022;419-434. ‏ Joseph J, N., Shrivastava, A., Benny, B., Baig, M. Y., Georgine S, A., & Saral A, M. (2023). Antiviral properties of various bioactive components present in the root of Glycyrrhiza glabra. Current Nutrition & Food Science , 19(2), 166-175. ‏ Parizipour MG, Shahriari AG. Investigation of antiviral potential of licorice ( Glycyrrhiza glabra L.) crude extract against Tobacco mosaic virus . J. Anim. Plant Sci, 2020;30(1):107-114. ‏ Gomaa AA, Abdel-Wadood YA. The potential of glycyrrhizin and licorice extract in combating COVID-19 and associated conditions. Phytomedicine plus, 2021;1(3):1-12. ‏ Elshaer NA, El-Masry SS, Rabiee MS, Sadik AS, Megahed AA. In Silico prediction of the potential of some bioactive compounds from Licorice to target Banana bunchy top virus . Egyptian Journal of Phytopathology, 2025;53(1):194-224. Jakhar R, Dangi M, Khichi A, Chhillar AK. Relevance of molecular docking studies in drug designing. Current Bioinformatics, 2020; 15 (4):270-278. ‏ Mahmud S, Uddin MAR, Paul GK, Shimu MSS, Islam S, Rahman E, et al. Virtual screening and molecular dynamics simulation study of plant-derived compounds to identify potential inhibitors of main protease from SARS-CoV-2. Briefings in bioinformatics, 2021;22(2):1402-1414. ‏ Jamal QMS. Antiviral potential of plants against COVID-19 during outbreaks-An update. International Journal of Molecular Sciences, 2022;23(21):1-25. ‏ Hýsková V, Bělonožníková K, Chmelík J, Hoffmeisterová H, Čeřovská N, Moravec T, et al. Potyviral helper-component protease: Multifaced functions and interactions with host proteins. Plants, 2024;13(9):1236. ‏ https://doi.org/10.3390/plants13091236 Gohlke H, Klebe G. Approaches to the description and prediction of the binding affinity of small‐molecule ligands to macromolecular receptors. Angewandte Chemie International Edition, 2002;41(15):2644-2676. ‏ Aseel DG, Rabie M, El-Far A, Abdelkhalek A. Antiviral properties and molecular docking studies of eco-friendly biosynthesized copper oxide nanoparticles against alfalfa mosaic virus. BMC Plant Biology, 2024;24(1):1-16. ‏ https://link.springer.com/article/10.1186/s12870-024-05802-1 Kitchen DB, Decornez H, Furr JR, Bajorath J. Docking and scoring in virtual screening for drug discovery: Methods and applications. Nature reviews Drug discovery, 2004;3(11):935-949. ‏ Khan T, Raza S. Exploration of computational aids for effective drug designing and management of viral diseases: A comprehensive review. Current Topics in Medicinal Chemistry, 2023;23(17):1640-1663. ‏ Kirchmair J, Distinto S, Roman Liedl K, Markt P, Maria Rollinger J, Schuster D, et al. Development of anti-viral agents using molecular modeling and virtual screening techniques. Infectious Disorders-Drug Targets (Formerly Current Drug Targets-Infectious Disorders), 2011;11(1):64-93. ‏ Azeem M, Mustafa G, Ahmed S, Mushtaq A, Arshad M, Usama M, et al. Structure based screening and molecular docking with dynamic simulation of natural secondary metabolites to target RNA-dependent RNA polymerase of five different retroviruses. Plos one, 2024;19(8):e0307615. ‏ https://doi.org/10.1371/journal.pone.0307615 Bai Q, Jiang J, Luo D, Huang Y, Huang M, Zhao G, et al. Cysteine protease domain of Potato Virus Y: The potential target for urea derivatives. pestic. biochem. Physiol., 189, 2023;105309. https://doi.org/10.1016/j.pestbp.2022.10530 Ballester PJ, Mitchell JB. A machine learning approach to predicting protein–ligand binding affinity with applications to molecular docking. Bioinformatics, 2010;26(9):1169-1175. ‏ https://doi.org/10.1093/bioinformatics/btq112 Choudhury C, Narahari Sastry G. Pharmacophore modelling and screening: Concepts, recent developments and applications in rational drug design. Structural bioinformatics: applications in preclinical drug discovery process, 2019;25-53. ‏ Brylinski M. Aromatic interactions at the ligand–protein interface: Implications for the development of docking scoring functions. Chemical biology & drug design, 2018;91(2):380-390. ‏ https://doi.org/10.1111/cbdd.13084 Wang X, Song K, Li L, Chen L. Structure-based drug design strategies and challenges. Current Topics in Medicinal Chemistry, 2018;18(12):998-1006. ‏ de Sousa Luis JA, Barros RP, de Sousa NF, Muratov E, Scotti L, Scotti MT. Virtual screening of natural products database. Mini Reviews in Medicinal Chemistry, 2021;21(18):2657-2730. ‏ Ghildiyal R, Prakash V, Chaudhary VK, Gupta V, Gabrani R. Phytochemicals as antiviral agents: Recent updates. Plant-Derived Bioactives: Production, Properties and Therapeutic Applications, 2020;279-295. ‏ Liu L, Bagal D, Kitova EN, Schnier PD, Klassen JS. Hydrophobic protein−ligand interactions preserved in the gas phase. Journal of the American Chemical Society, 2009;131(44):15980-15981. ‏ Li T, Ayers PW, Liu S, Swadley MJ, Aubrey‐Medendorp C. Crystallization force—a density functional theory concept for revealing intermolecular interactions and molecular packing in organic crystals. Chemistry–A European Journal, 2009;15(2):361-371. ‏ Tables Table 1 Molecular docking and binding affinities of four licorice compounds against ZYMV protein. Ligands ZYMV-protein P1 HC-Pro P3 6K1 CI 6K2 NIa-VPg NIa-Pro NIb CP Molecular docking Glycyrrhetic acid -9.4 -7.1 -6.1 -7.1 -8.4 -6.4 -7.3 -8.1 -8.8 -6.4 Isoliquiritin -8.6 -7.0 -6.2 -6.3 -8.3 -5.8 -8.7 -7.8 -7.8 -6.3 Liquiritin -9.6 -7.0 -6.3 -6.6 -9.2 -6.1 -7.8 -8.3 -8.5 -6.5 Glabridin -8.8 -6.6 -6.2 -6.6 -8.3 -6.7 -8.8 -8.1 -8.7 -6.3 Control Acyclovir -6.2 -5.2 -5.6 -4.5 -5.8 -3.9 -5.2 -5.7 -5.3 -4.6 Binding affinities Glycyrrhetic acid -9.5 -7.5 -6.0 -7.0 -8.7 -6.5 -7.3 -8.1 -9.0 -6.9 Isoliquiritin -8.5 -7.1 -6.2 -6.3 -8.1 -5.5 -8.4 -7.7 -7.6 -6.2 Liquiritin -9.5 -7.2 -6.7 -6.3 -8.8 -6.1 -7.1 -8.2 -8.2 -6.4 Glabridin -9.0 -6.6 -6.2 -6.6 -8.4 -6.1 -8.8 -8.1 -8.4 -6.3 Control Acyclovir -6.3 -5.6 -5.7 -4.6 -5.9 -3.8 -4.4 -5.9 -5.5 -4.4 Table 2 Bonding Interactions of Amino Acid Residues in ZYMV-P1 Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-P1 GLY A:1447 Conventional Hydrogen, Conventional Hydrogen THR A:1472 Conventional Hydrogen THR A:1278 Conventional Hydrogen VAL A:1345 Alkyl, Alkyl LYS A:1492 Alkyl VAL A:1493 Alkyl Isoliquiritin-ZYMV-P1 GLU A:1805 Conventional Hydrogen ARG A:1505 Conventional Hydrogen, Pi-Alkyl VAL A:1806 Pi-Alkyl TYR A:1754 Conventional Hydrogen LYS A:1803 Unfavorable Acceptor-Acceptor GLN A:1801 Conventional Hydrogen, Conventional Hydrogen Liquiritin-ZYMV-P1 PHE A:1633 Conventional Hydrogen SER A:1807 Carbon- H HIS A:1631 Pi-Pi Stacked LEU A:1786 Pi-Sigma SER A:1635 Conventional Hydrogen ASP A:1429 Unfavorable Donor-Donor LYS A:1433 Conventional Hydrogen, Unfavorable Acceptor-Acceptor Glabridin-ZYMV-P1 ASN A:1426 Conventional Hydrogen, Conventional Hydrogen HIS A:1631 Alkyl, Pi-Pi Stacked, Pi-Alkyl, Alkyl LEU A:1786 Pi-Alkyl, Pi-Alkyl, Alkyl PHE A:1660 Alkyl PHE A:1633 Carbon- H Notes: ZYMV-P1: Zucchini yellow mosaic virus-P1; GLY: Glycine; THR: Threonine; VAL: Valine; LYS: Lysine; GLU: Glutamic acid; ARG: Arginine; TYR: Tyrosine; GLN: Glutamine; PHE: Phenylalanine; SER: Serine; HIS: Histidine; LEU : Leucine; ASP: Aspartic acid; and ASN: Asparagine. Table 3 Bonding Interactions of Amino Acid Residues in ZYMV-HC-Pro Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-HC-Pro CYS A:342 Alkyl ILE A:417 Alkyl, Alkyl, Carbon- H TYR A:335 Conventional Hydrogen ALA A:337 Alkyl, Alkyl, Alkyl Isoliquiritin-ZYMV-HC-Pro VAL A:352 Pi-Alkyl TYR A:335 Conventional Hydrogen ALA A:432 Carbon Hydrogen LEU A:430 Conventional Hydrogen, Conventional Hydrogen ALA A:349 Conventional Hydrogen GLU A:401 Conventional Hydrogen, Pi-Anion, PI Sigma Liquiritin-ZYMV-HC-Pro TYR A:335 Conventional Hydrogen HIS A:415 Unfavorable Donor-Donor GLY A:456 Conventional Hydrogen VAL A:416 Conventional Hydrogen CYS A:342 Pi-Sulfur ILE A:417 Pi-Sigma Glabridin-ZYMV-HC-Pro SER A:419 Conventional Hydrogen GLU A:401 Pi-Anion ASP A:418 Pi-Anion ALA A:349 Pi-Alkyl VAL A:352 Alkyl, Alkyl PRO A:403 Carbon Hydrogen ARG A:404 Pi-Alkyl, Conventional Hydrogen Notes: ZYMV-HC-Pro: Zucchini yellow mosaic virus-HC-Pro; CYS: Cysteine; ILE: Isoleucine; TYR: Tyrosine; ALA: Alanine; VAL: Valine; LEU : Leucine; GLU: Glutamate; HIS: Histidine; GLY: Glycine; SER: Serine; ASP: Aspartic acid ; PRO: Proline; and ARG: Arginine. Table 4 Bonding Interactions of Amino Acid Residues in ZYMV-P3 Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-P3 HIS A:304 Carbon Hydrogen, Pi-Alkyl ILE A:305 Alkyl, Alkyl SER A:307 Conventional Hydrogen HIS A:322 Alkyl, Pi-Sigma, Carbon Hydrogen ARG A:327 Pi-Alkyl Isoliquiritin-ZYMV-P3 ASP A:329 Conventional Hydrogen ARG A:327 Unfavorable Donor-Donor ILE A:305 Pi-Sigma HIS A:322 Pi-Pi Stacked ASN A:325 Unfavorable Donor-Donor Liquiritin-ZYMV-P3 SER A:307 Conventional Hydrogen HIS A:322 Carbon Hydrogen, Pi-Pi Stacked ARG A:327 Conventional Hydrogen ILE A:305 Pi-Alkyl Glabridin-ZYMV-P3 ARG A:327 Pi-Alkyl, Pi-Alkyl, Alkyl ASP A:329 Pi-Anion ILE A:305 Pi-Alkyl, Alkyl, Carbon Hydrogen HIS A:322 Conventional Hydrogen, Pi-Pi Stacked ASN A:325 Conventional Hydrogen, Unfavorable Donor-Donor Notes: ZYMV-P3: Zucchini yellow mosaic virus-P3; HIS: Histidine; ILE: Isoleucine; SER: Serine; ARG: Arginine; ASP: Aspartic acid; and ASN: Asparagine. Table 5 Bonding Interactions of Amino Acid Residues in ZYMV-6K1 Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-6K1 PHE A:23 Alkyl ILE A:34 Alkyl, Pi-Alkyl, Conventional Hydrogen PHE A:32 Pi-Alkyl Isoliquiritin-ZYMV-6K1 ASP A:24 Conventional Hydrogen ARG A:27 Conventional Hydrogen PHE A:23 Pi-Pi T-Shaped ILE A:34 Pi-Sigma Liquiritin-ZYMV-6K1 LYS A:37 Unfavorable Donor-Donor ARG A:27 Conventional Hydrogen PHE A:23 Pi-Pi T-Shaped ILE A:34 Pi-Sigma Glabridin-ZYMV-6K1 ILE A:34 Pi-Sigma VAL A:41 Pi-Alkyl LEU A:38 Pi-Alkyl, Pi-Alkyl VAL A:15 Alkyl, Pi-Alkyl LYS A:37 Alkyl, Alkyl, Pi-Alkyl, Pi-Alkyl, Pi-Cation LEU A:16 Pi-Alkyl, Pi-Alkyl, Alkyl LEU A:35 Conventional Hydrogen Notes: ZYMV-6K1: Zucchini yellow mosaic virus-6K1; PHE: Phenylalanine; ILE: Isoleucine; ASP: Aspartic acid; ARG: Arginine; LYS: Lysine; VAL; Valine; and LEU : Leucine. Table 6 Bonding Interactions of Amino Acid Residues in ZYMV-CI Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-CI PRO A:207 Pi-Alkyl THR A:179 Carbon Hydrogen SER A:376 Carbon Hydrogen PRO A:378 Pi-Alkyl, Pi-Alkyl, Pi-Alkyl HIS A:177 Carbon Hydrogen THR A:205 Pi-Donor-H, Carbon Hydrogen Isoliquiritin-ZYMV-CI THR A:205 Pi-Donor-H PRO A:207 Pi-Alkyl SER A:376 Conventional Hydrogen ARG A:209 Unfavorable Donor-Donor ASN A:187 Conventional Hydrogen, Unfavorable Donor-Donor Liquiritin-ZYMV-CI GLY A:208 Conventional Hydrogen, Pi-Donor-H PRO A:207 Pi-Alkyl THR A:205 Pi-Donor-H ASN A:310 Unfavorable Donor-Donor ASN A:187 Unfavorable Donor-Donor Glabridin-ZYMV-CI PRO A:207 Alkyl THR A:179 Pi-Donor-H SER A:376 Pi-Donor-H PRO A:378 Pi-Alkyl, Pi-Alkyl, Pi-Sigma HIS A:177 Carbon Hydrogen THR A:205 Pi-Donor-H, Carbon Hydrogen Notes: ZYMV-CI: Zucchini yellow mosaic virus-CI; PRO: Proline; THR: Threonine; SER: Serine; HIS: Histidine; ARG: Arginine; ASN: Asparagine; and GLY; Glycine Table 7 Bonding Interactions of Amino Acid Residues in ZYMV-6K2 Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-6K2 TRP D:36 Pi-Alkyl, Pi-Alkyl, Pi-Alkyl Isoliquiritin-ZYMV-6K2 ASN D:22 Conventional Hydrogen, Unfavorable Donor-Donor TRP D:15 Pi-Pi Stacked LYS D:19 Pi-Alkyl, Pi-Alkyl ASP D:23 Pi-Anion, Conventional Hydrogen, Unfavorable Donor-Donor Liquiritin-ZYMV-6K2 GLY D:33 van der Waals MET D: 29 Pi-Alkyl LEU D:32 Amide-Pi Stacked, Amide-Pi Stacked Glabridin-ZYMV-6K2 LYS D:19 Pi-Alkyl, Alkyl TRP D:15 Pi-Alkyl, Alkyl, Alkyl, Pi-Pi Stacked Notes: ZYMV-6K2: Zucchini yellow mosaic virus-6K2; TRP: Tryptophan; ASN: Asparagine; LYS: Lysine; ASP: Aspartic acid; GLY; Glycine; MET: Methionine; and LEU : Leucine. Table 8 Bonding Interactions of Amino Acid Residues in ZYMV-NIa-VPg Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-NIa-VPg PRO A:143 Carbon Hydrogen, Alkyl VAL A:96 Alkyl ILE A:93 Alkyl, Alkyl, Alkyl ILE A:124 Alkyl, Alkyl LEU A:141 Alkyl, Alkyl Isoliquiritin-ZYMV-NIa-VPg ASP A:78 Conventional Hydrogen THR A:91 Unfavorable Acceptor-Acceptor THR A:89 Conventional Hydrogen ILE A:124 Pi-Sigma, Pi-Alkyl Liquiritin-ZYMV-NIa-VPg LYS A:121 Conventional Hydrogen ASP A:78 Conventional Hydrogen LEU A:141 Pi-Sigma ILE A:124 Pi-Sigma VAL A:96 Pi-Alkyl ILE A:93 Pi-Alkyl Glabridin-ZYMV-NIa-VPg LEU A:141 Pi-Alkyl ILE A:124 Alkyl, Pi-Alkyl, Pi-Alkyl, Pi-Sigma ILE A:93 Alkyl, Pi-Alkyl, Pi-Sigma VAL A:96 Pi-Alkyl Notes: ZYMV-NIa-VPg: Zucchini yellow mosaic virus-NIa-VPg; PRO: Proline; VAL; Valine; ILE: Isoleucine; LEU : Leucine; ASP: Aspartic acid; THR: Threonine; and LYS: Lysine. Table 9 Bonding Interactions of Amino Acid Residues in ZYMV-NIa-Pro Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-NIa-Pro LYS A:6 Conventional Hydrogen TYR A:11 Conventional Hydrogen VAL A:125 Alkyl, Alkyl TYR A:5 Pi-Alkyl Isoliquiritin-ZYMV-NIa-Pro ALA A:170 Pi-Sigma, Conventional Hydrogen GLY A:168 Conventional Hydrogen LYS A:29 Unfavorable Acceptor-Acceptor THR A:146 Conventional Hydrogen Liquiritin-ZYMV-NIa-Pro GLU A:220 Unfavorable Acceptor-Acceptor GLU A:30 Conventional Hydrogen ALA A:170 Pi-Alkyl CYS A:151 Pi-Alkyl ASN A:147 Conventional Hydrogen THR A:146 Conventional Hydrogen GLN A:221 Conventional Hydrogen LYS A:29 Conventional Hydrogen, Conventional Hydrogen Glabridin-ZYMV-NIa-Pro GLU A:148 Pi-Anion ALA A:170 Pi-Alkyl Notes: ZYMV-NIa-Pro: Zucchini yellow mosaic virus-Nia-Pro; LYS: Lysine; TYR: Tyrosine; VAL; Valine; ALA: Alanine; GLY; Glycine; THR: Threonine; GLU: Glutamic acid; CYS: Cysteine; ASN: Asparagine; and GLN: Glutamine Table 10 Bonding Interactions of Amino Acid Residues in ZYMV-NIb Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-NIb LEU A:122 Alkyl LEU A:152 Alkyl SER A:121 Conventional Hydrogen VAL A:202 Alkyl CYS A:203 Conventional Hydrogen MET A:281 Alkyl TYR A:119 Pi-Sigma PHE A:140 Pi-Alkyl, Pi-Alkyl ARG A:148 Unfavorable Donor-Donor LYS A:135 Conventional Hydrogen LEU A:198 Pi-Alkyl, Alkyl Isoliquiritin-ZYMV-NIb THR A:81 Pi-Sigma ASN A:184 Conventional Hydrogen, Conventional Hydrogen SER A:254 Unfavorable Donor-Donor ASP A:253 Conventional Hydrogen ASP A:352 Conventional Hydrogen ARG A:187 Pi-Alkyl, Conventional Hydrogen LYS A:185 Pi-Alkyl Liquiritin-ZYMV-NIb GLU A:116 Carbon Hydrogen ILE A:118 Carbon Hydrogen SER A:121 Conventional Hydrogen LEU A:198 Pi-Sigma TYR A:119 Pi-Pi T-Shaped VAL A:202 Pi-Alkyl VAL A:204 Carbon Hydrogen ASP A:205 Carbon Hydrogen ASP A:206 Conventional Hydrogen PHE A:207 Carbon Hydrogen, Conventional Hydrogen Glabridin-ZYMV-NIb SER A:310 Conventional Hydrogen ARG A:187 Alkyl, Alkyl LYS A:185 Alkyl, Alkyl LYS A:304 Conventional Hydrogen Notes: ZYMV-NIb: Zucchini yellow mosaic virus-NIb; LEU : Leucine; SER: Serine; VAL; Valine; CYS: Cysteine; MET: Methionine; TYR: Tyrosine; PHE: Phenylalanine; ARG: Arginine; LYS: Lysine; GLU: Glutamic acid; THR: Threonine; ASN: Asparagine; ASP: Aspartic acid; ARG: Arginine; and PHE: Phenylalanine. Table 11 Bonding Interactions of Amino Acid Residues in ZYMV-CP Protein with Four Licorice-Derived Bioactive Compounds. Amino acids Sites Types of bonds Glycyrrhetic acid-ZYMV-CP ALA B:39 Alkyl, Pi-Alkyl LYS C:44 Conventional Hydrogen PHE C:36 Alkyl LYS C:34 Alkyl Isoliquiritin-ZYMV-CP LYS C:41 Pi-Alkyl PRO C:38 Conventional Hydrogen ARG C:42 Unfavorable Donor-Donor LYS C:44 Pi-Alkyl, Conventional Hydrogen, Pi-Anion ASP C:30 Pi-Cation LEU C:29 Pi-Sigma Liquiritin-ZYMV-CP ARG C:23 Unfavorable Donor-Donor, Conventional Hydrogen ASN B:37 Conventional Hydrogen PHE C:31 Conventional Hydrogen ALA B:39 Pi-Alkyl ARG B:42 Conventional Hydrogen GLU C:26 Conventional Hydrogen, Conventional Hydrogen, Carbon Hydrogen Glabridin-ZYMV-CP ALA A:39 Pi-Sigma, Alkyl ASP B:30 Conventional Hydrogen, Pi-Cation ARG A:42 Pi-Anion ALA B:27 Pi-Alkyl PRO A:38 Pi-Alkyl Notes: ZYMV-CP: Zucchini yellow mosaic virus-CP; ALA, Alanine; LYS, Lysine; PHE, Phenylalanine; PRO: Proline; ARG: Arginine; ASP: Aspartic acid; LEU : Leucine; ARG: Arginine; ASN: Asparagine; PHE: Phenylalanine); and GLU: Glutamic Acid (Glutamate) Figures The cited figures are not available with this version. Additional Declarations No competing interests reported. Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-7011143","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":482474899,"identity":"0768e08c-6a3e-47c1-beeb-5035176eca3b","order_by":0,"name":"Shrouk E.E. Farag","email":"","orcid":"","institution":"Department of Agricultural Microbiology, Laboratory of Virology, Faculty of Agriculture, Ain Shams University, P.O. Box 68, Hadayek Shobra, Cairo, Egypt","correspondingAuthor":false,"prefix":"","firstName":"Shrouk","middleName":"E.E.","lastName":"Farag","suffix":""},{"id":482474900,"identity":"bcf16dab-de0c-4707-a1cc-cef8e487d1cc","order_by":1,"name":"Shafik D. Ibrahim","email":"","orcid":"","institution":"Agricultural Genetic Engineering Research Institute, Agricultural Research Center, 9 Gamaa St., P.O. Box, 12619, Giza, Egypt","correspondingAuthor":false,"prefix":"","firstName":"Shafik","middleName":"D.","lastName":"Ibrahim","suffix":""},{"id":482474901,"identity":"22a06661-1192-4868-9799-70b7992dbc27","order_by":2,"name":"Atef S. Sadik","email":"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA4klEQVRIiWNgGAWjYJCCD0DM2MbDfICBsYEY9WwMjDMgWtgSSNTSwMNjQJwW/vnNBxsY/tjJ9vGc+Sbxc4eNHAP74aMb8GmROMaW2MDYlmzcxtu7TbL3TJoxA09a2g281hzjMX/A2MCc2MbPu02Ct+1wYoMEjxleLfLH+D8CHVYP1MLzTPIvMVoMjvEA/cx2OLGNt4dNmihbDI+lGQL9cty4jeeYsbVsW5oxGyG/yB0+/BDosGrZ+T3JD2++bbOR42c/fAy/94GA+Q+EZpEAkWyElKNo/UCK6lEwCkbBKBg5AABy3Ul76XU/9AAAAABJRU5ErkJggg==","orcid":"","institution":"Department of Agricultural Microbiology, Laboratory of Virology, Faculty of Agriculture, Ain Shams University, P.O. Box 68, Hadayek Shobra, Cairo, Egypt","correspondingAuthor":true,"prefix":"","firstName":"Atef","middleName":"S.","lastName":"Sadik","suffix":""},{"id":482474902,"identity":"3673c74d-ef5e-4995-86d8-753d9335173a","order_by":3,"name":"Mamdouh H. Abdel-Gaffar","email":"","orcid":"","institution":"Department of Agricultural Microbiology, Laboratory of Virology, Faculty of Agriculture, Ain Shams University, P.O. Box 68, Hadayek Shobra, Cairo, Egypt","correspondingAuthor":false,"prefix":"","firstName":"Mamdouh","middleName":"H.","lastName":"Abdel-Gaffar","suffix":""}],"badges":[],"createdAt":"2025-06-30 13:38:26","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-7011143/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-7011143/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":87931572,"identity":"23615ef4-62bc-4386-b123-57c0785994a9","added_by":"auto","created_at":"2025-07-30 13:39:42","extension":"pdf","order_by":0,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1769024,"visible":true,"origin":"","legend":"","description":"","filename":"manuscript.pdf","url":"https://assets-eu.researchsquare.com/files/rs-7011143/v1/ae3ba493-8e80-433e-8345-8fdbfff24b96.pdf"}],"financialInterests":"No competing interests reported.","formattedTitle":"Assessment of Antiviral Activities of Four Licorice Compounds against Zucchini Yellow Mosaic Virus through Molecular Docking","fulltext":[{"header":"Introduction","content":"\u003cp\u003eZucchini Yellow Mosaic Virus (ZYMV) is a significant viral pathogen affecting cucurbit crops, particularly zucchini, leading to substantial yield losses worldwide [1]. Transmitted by aphids, ZYMV causes symptoms such as yellowing of leaves, mosaic patterns, and stunted growth, severely impacting crop quality and yield [2]. Traditional control measures, including chemical pesticides and resistant cultivars, are often ineffective, environmentally damaging, or economically unsustainable [3, 4]. This has prompted an increased interest in exploring alternative, eco-friendly solutions for managing viral diseases in crops [5, 6].\u003c/p\u003e\n\u003cp\u003eLicorice (\u003cem\u003eGlycyrrhiza glabra\u003c/em\u003e), a plant renowned for its medicinal properties, has shown potential as a source of antiviral agents. Its bioactive compounds, including glycyrrhizin, flavonoids, and triterpenoids, are known for their antiviral, anti-inflammatory, and immune-modulating activities [7]. These compounds have demonstrated effectiveness against a variety of human and plant viruses [8-10].\u003c/p\u003e\n\u003cp\u003eRecent advancements in computational tools, particularly molecular docking, have enabled researchers to predict and analyze the interactions between bioactive compounds and viral proteins. Molecular docking offers a powerful, cost-effective method to screen potential antiviral agents by simulating the binding of compounds to critical viral proteins, such as the coat protein\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e(CP) and RNA-dependent RNA polymerase (RdRp), which play key roles in the replication and infectivity of plant viruses [11-14].\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eMolecular docking\u003c/strong\u003e has become an invaluable tool in the study of plant viruses, particularly in the identification of potential antiviral compounds. By simulating the interactions between small molecules and viral proteins, molecular docking allows researchers to predict how these compounds may inhibit viral replication, thus offering a promising alternative to traditional experimental approaches [15, 16]. This technique allows for the identification of compounds with strong binding affinities to viral proteins, suggesting their potential for inhibiting viral replication [17].\u003c/p\u003e\n\u003cp\u003eThis computational technique is especially useful in the context of plant viruses, where effective antiviral agents are limited [18]. It enables the identification of key viral proteins, such as coat proteins or RNA-dependent RNA polymerases, which are critical for the virus\u0026rsquo;s replication and infectivity [19]. Docking studies can also reveal the precise binding sites and interactions between bioactive compounds-often derived from plants themselves-and these viral proteins [20]. \u0026nbsp;\u003c/p\u003e\n\u003cp\u003eMolecular docking studies have revealed that ASP 121, ASN 48, and TYR 38 are key sites of interaction between the PVY HC-Pro C-terminal domain and these compounds. These amino acid residues are critical for the design and synthesis of novel urea derivatives as potential antiviral agents [21]. This in silico approach enables the identification of promising compounds from licorice that could inhibit viral replication and reduce the severity of disease symptoms in infected crops.\u003c/p\u003e\n\u003cp\u003eThe objective of this study is to evaluate the antiviral activities of four licorice-derived compounds-glycyrrhizin, liquiritigenin, isoliquiritigenin, and glabridin-against ZYMV using molecular docking analysis. Through this computational approach, we aim to identify the most promising compounds that could be further explored for the development of antiviral agents against ZYMV. The findings from this study could contribute to the development of more sustainable and effective strategies for managing viral diseases in cucurbit crops.\u003c/p\u003e"},{"header":"Materials and Methods","content":"\u003ch4\u003e\u003cstrong\u003eSelected compounds for docking analysis\u003c/strong\u003e\u003c/h4\u003e\n\u003cp\u003eFour bioactive compounds (Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin) derived from Licorice were selected for assessment their antiviral activities against the proteins encoded from the ten genes of the genome of an Egyptian strain of ZYMV documented in GenBank under accession number of LC795783.1 using molecular docking tool. Their chemical structures were retrieved in 2D SDF format from the \u003cstrong\u003ePubChem database\u003c/strong\u003e[https://pubchem.ncbi.nlm.nih.gov/].\u003c/p\u003e\n\u003ch4\u003e\u003cstrong\u003ePreparation of ZYMV Proteins \u003c/strong\u003e\u003c/h4\u003e\n\u003cp\u003eThe ZYMV proteins [P1 (Accession: BFF82028.1), HC-Pro (Accession: BFF82029.1), P3 (Accession: BFF82030.1), 6k1 (Accession: BFF82031.1), CI (Accession: BFF82032.1), 6K2 (Accession: BFF82033.1), NIa-VPg (Accession: BFF82034.1), NIb-Pro (Accession: BFF82035.1), NIb (Accession: BFF82036.1), and CP (Accession: BFF82037.1)] were retrieved in FASTA format from the \u003cstrong\u003eNCBI database\u003c/strong\u003e [https://www.ncbi.nlm.nih.gov]. To obtain the 3D structures of the target proteins in PDB format, a search was performed on the Protein Data Bank (PDB) website [https://www.rcsb.org/]. In cases where the structures were unavailable, 3D models of the proteins were generated through homology modeling, using sequence alignments to known structures, with tools such as SWISS-MODEL or Phyre2. \u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eVirtual Screening of Bioactive Compounds\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eA library of bioactive compounds was compiled for virtual screening. The screening was conducted using PyRx software [https://sourceforge.net/projects/pyrx/], which combines energy minimization with docking simulations through the AutoDock Vina plugin. The compounds were docked against the replicase and coat protein of PVX to prioritize those exhibiting lower binding energy values, suggesting stronger binding potential. The 2D molecular structures were converted to 3D forms and optimized for energy minimization using tools like Open Babel and Chem3D.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eMolecular Docking\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe docking process involved several preparatory steps. Target proteins were processed by removing water molecules and irrelevant ligands using PyMOL. Hydrogen atoms were added, and either Kollman or Gasteiger charges were assigned to the protein. The ligands were energy-minimized using Open Babel or Chem3D to ensure optimal geometry for the docking process. Docking simulations were carried out with CB-Dock and AutoDock Vina. The binding affinities (in kcal/mol) of each protein-ligand complex were recorded. CB-Dock facilitated the automatic identification of potential binding sites, ensuring more accurate docking results.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eVisualization and Analysis\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe results of the docking simulations were analyzed and visualized using Discovery Studio 2022 [https://10.0.142.116/Pharmaceutical-Sciences.543] to examine key interactions such as hydrogen bonds, hydrophobic contacts, and ionic interactions between the protein and the ligands.\u003c/p\u003e"},{"header":"Results","content":"\u003cp\u003eThe data presented in\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003eTable 1\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003eprovides insights into the molecular docking and binding affinities of four licorice-derived bioactive compounds-Glabridin, Glycyrrhetic acid, Isoliquiritin, and Liquiritin-against various ZYMV protein targets, including P1, HC-Pro, P3, and others. The table also compares these compounds to the control drug, Acyclovir.\u003c/p\u003e\n\u003cp\u003eGlabridin shows moderate binding across all targets, with docking scores ranging from -6.3 to -8.8. This suggests that Glabridin can effectively bind to the ZYMV protein targets, though it may not exhibit the strongest binding compared to the other compounds. Glycyrrhetic acid demonstrates relatively consistent docking scores, ranging from -6.1 to -9.4, indicating favorable binding with most ZYMV protein targets. It achieves the lowest docking score against the P1 target (-9.4), suggesting strong binding in this case. Isoliquiritin shows docking scores ranging from -5.8 to -8.7, indicating a weaker binding profile overall. Its best binding score is with the NIa-VPg target (-8.7), but it also demonstrates relatively weaker interactions with other targets like P3 (-6.2) and 6K1 (-5.8). Liquiritin presents docking scores ranging from -6.1 to -9.6, indicating promising binding interactions across multiple targets. Its best interaction is seen with the P1 target (-9.6), similar to Glycyrrhetic acid, highlighting its strong potential as a ZYMV inhibitor. Acyclovir, the control drug, shows generally weaker docking scores compared to the licorice compounds, with values ranging from -3.8 to -6.3, indicating that it binds less effectively to the ZYMV proteins compared to the licorice compounds.\u003c/p\u003e\n\u003cp\u003eThe data presented (Table 2\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e\u0026nbsp;\u003c/span\u003e\u003c/strong\u003e\u0026amp; Fig. 1) reveals the variety of bonding interactions that occur between the ligands and the amino acid residues of the protein. Conventional hydrogen bonds are the most common form of interaction, helping to stabilize the protein-ligand complexes. Alkyl and Pi-Alkyl interactions also feature prominently, highlighting the role of hydrophobic and aromatic stacking interactions in binding affinity. In some cases, the dataset points to unfavorable interactions, such as donor-donor and acceptor-acceptor bonds, which could inform future modifications to improve ligand binding or optimize the overall interaction profile. These unfavorable interactions might also provide insight into areas where ligand optimization could be beneficial to enhance stability or specificity in targeting the protein.\u003c/p\u003e\n\u003cp\u003eThe presence of diverse bonding types, including hydrogen, alkyl, and pi-based interactions, reflects the complex nature of protein-ligand binding and offers valuable information for understanding how these bioactive compounds interact with the ZYMV-P1 protein. This analysis could inform future research on drug design, specifically in targeting ZYMV or similar viruses, and may even contribute to the development of more effective antiviral compounds based on licorice-derived molecules. Overall, the title and the associated results emphasize the importance of understanding the molecular interactions that underlie potential therapeutic interventions.\u003c/p\u003e\n\u003cp\u003eThe results presented in Table (3\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e\u0026nbsp;\u003c/span\u003e\u003c/strong\u003e\u0026amp; Fig. 2) highlight the bonding interactions between various amino acid residues in the ZYMV-HC-Pro protein and four licorice-derived bioactive compounds: Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin. The data reveals a diverse array of interaction types, including conventional hydrogen bonds, alkyl interactions, pi-stacking, and more specialized bonds like Pi-Anion and Pi-Sulfur interactions.\u003c/p\u003e\n\u003cp\u003eFor\u0026nbsp;\u003cstrong\u003eGlycyrrhetic acid\u003c/strong\u003e\u003cstrong\u003e,\u003c/strong\u003e the interactions are primarily hydrophobic, with alkyl bonds playing a significant role in stabilizing the complex at sites such as CYS A:342, ALA A:337, and ILE A:417. Conventional hydrogen bonds are also present at TYR A:335, reinforcing the structural integrity of the binding. The presence of multiple alkyl interactions at ALA A:337, in particular, indicates a strong hydrophobic environment, likely contributing to the stabilization of the ligand within the protein\u0026rsquo;s binding site.\u003c/p\u003e\n\u003cp\u003eIn the case of\u0026nbsp;\u003cstrong\u003eIsoliquiritin\u003c/strong\u003e, several notable pi-based interactions are observed, such as the Pi-Alkyl interaction at VAL A:352, which suggests a strong aromatic interaction, likely aiding the binding affinity. TYR A:335, ALA A:349, and LEU A:430 exhibit conventional hydrogen bonds, contributing to a stable protein-ligand interface. Additionally, GLU A:401 shows a more complex bonding pattern, involving conventional hydrogen bonds, as well as Pi-Anion and Pi-Sigma interactions, which could indicate a more sophisticated interaction mode with this ligand.\u003c/p\u003e\n\u003cp\u003eFor\u0026nbsp;\u003cstrong\u003eLiquiritin\u003c/strong\u003e, the interaction profile is again diverse, with conventional hydrogen bonds predominating, such as those at TYR A:335, GLY A:456, and VAL A:416. Interestingly, HIS A:415 shows an\u0026nbsp;\u003cstrong\u003eunfavorable donor-donor\u003c/strong\u003e interaction, which could suggest potential areas where the binding is less stable or where further ligand optimization might improve affinity. Furthermore, CYS A:342 engages in a\u0026nbsp;\u003cstrong\u003ePi-Sulfur\u003c/strong\u003e interaction, which is notable for its role in stabilizing the ligand through sulfur-aromatic interactions, commonly seen in enzyme-inhibitor complexes. ILE A:417 also exhibits a\u0026nbsp;\u003cstrong\u003ePi-Sigma\u003c/strong\u003e interaction, further highlighting the contribution of aromatic stacking in binding.\u003c/p\u003e\n\u003cp\u003eFinally,\u0026nbsp;\u003cstrong\u003eGlabridin\u003c/strong\u003e shows a combination of both conventional hydrogen bonds and more specialized interactions. For example, SER A:419 forms conventional hydrogen bonds, while GLU A:401 and ASP A:418 participate in Pi-Anion interactions, potentially involving electrostatic stabilization. ALA A:349 forms a\u0026nbsp;\u003cstrong\u003ePi-Alkyl\u003c/strong\u003e interaction, further suggesting that hydrophobic and aromatic interactions are key to binding. The presence of Pi-Alkyl and alkyl interactions at VAL A:352 and ARG A:404 also highlights a significant role of hydrophobic forces in stabilizing the interaction. Additionally, PRO A:403 exhibits a\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e\u003cstrong\u003ecarbon-hydrogen\u003c/strong\u003e interaction, contributing to the overall binding.\u003c/p\u003e\n\u003cp\u003eOverall, the variety of interaction types, including conventional hydrogen bonds, alkyl interactions, pi-stacking, and more specialized bonds like Pi-Anion and Pi-Sulfur, demonstrates the complexity of protein-ligand binding in the ZYMV-HC-Pro protein. These interactions suggest that licorice-derived compounds may effectively interact with the protein through a combination of hydrophobic, electrostatic, and aromatic interactions, providing valuable insights for further research into potential antiviral therapies.\u003c/p\u003e\n\u003cp\u003eData in Table (4\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e\u0026nbsp;\u003c/span\u003e\u003c/strong\u003e\u0026amp; Fig. 3) illustrates the bonding interactions between the amino acid residues in the ZYMV-P3 protein and four licorice-derived bioactive compounds: Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin. The interactions identified include a mixture of hydrophobic, hydrogen bonding, and aromatic interactions, each contributing to the stability and specificity of the protein-ligand binding.\u003c/p\u003e\n\u003cp\u003eFor\u0026nbsp;\u003cstrong\u003eGlycyrrhetic acid\u003c/strong\u003e, the interaction profile shows a strong presence of hydrophobic interactions, notably with\u0026nbsp;\u003cstrong\u003eAlkyl bonds\u003c/strong\u003e at ILE A:305 and HIS A:322. These alkyl interactions, especially when combined with the\u0026nbsp;\u003cstrong\u003ePi-Alkyl\u003c/strong\u003e bond at HIS A:304, indicate the importance of non-polar interactions in stabilizing the ligand-protein complex. The\u0026nbsp;\u003cstrong\u003ePi-Sigma\u003c/strong\u003e interaction at HIS A:322 further supports the aromatic stacking nature of the ligand\u0026apos;s binding. Conventional hydrogen bonds at SER A:307 and the\u0026nbsp;\u003cstrong\u003eCarbon-Hydrogen\u003c/strong\u003e interaction at HIS A:304 provide additional stabilization, ensuring a strong and diverse binding interface.\u003c/p\u003e\n\u003cp\u003eWith\u0026nbsp;\u003cstrong\u003eIsoliquiritin\u003c/strong\u003e\u003cstrong\u003e,\u003c/strong\u003e several unfavorable interactions are noted, particularly the\u0026nbsp;\u003cstrong\u003eunfavorable donor-donor\u003c/strong\u003e interactions at ARG A:327 and ASN A:325. These suggest that there may be some suboptimal binding in these regions, potentially due to steric clashes or electrostatic repulsion between the donor atoms. Despite these unfavorable interactions,\u0026nbsp;\u003cstrong\u003ePi-Sigma\u003c/strong\u003e interactions at ILE A:305 and\u0026nbsp;\u003cstrong\u003ePi-Pi stacking\u003c/strong\u003e at HIS A:322 highlight that aromatic interactions still play a key role in stabilizing the binding. The conventional hydrogen bond at ASP A:329 indicates a stabilizing interaction with polar residues, contributing to the overall binding.\u003c/p\u003e\n\u003cp\u003eFor\u0026nbsp;\u003cstrong\u003eLiquiritin\u003c/strong\u003e\u003cstrong\u003e,\u003c/strong\u003e the interactions are largely similar to those seen with Isoliquiritin, with\u0026nbsp;\u003cstrong\u003ePi-Pi stacking\u003c/strong\u003e at HIS A:322 and\u0026nbsp;\u003cstrong\u003ePi-Alkyl\u003c/strong\u003e at ILE A:305 continuing to demonstrate the importance of aromatic and hydrophobic interactions. The\u0026nbsp;\u003cstrong\u003econventional hydrogen bonds\u003c/strong\u003e at SER A:307 and ARG A:327 further reinforce the stability of the complex, suggesting that both hydrophobic and polar interactions are contributing to the overall affinity of the ligand for the protein.\u003c/p\u003e\n\u003cp\u003eFinally,\u0026nbsp;\u003cstrong\u003eGlabridin\u003c/strong\u003e presents a more complex interaction profile. The\u0026nbsp;\u003cstrong\u003ePi-Alkyl\u003c/strong\u003e and\u0026nbsp;\u003cstrong\u003eAlkyl\u003c/strong\u003e interactions at ARG A:327 and ILE A:305 suggest strong hydrophobic stabilizing forces, with multiple interactions at each site contributing to the overall binding. The\u0026nbsp;\u003cstrong\u003ePi-Anion\u003c/strong\u003e bond at ASP A:329 is another interesting feature, where electrostatic interactions likely enhance the stability of the binding at this site. Additionally,\u0026nbsp;\u003cstrong\u003ePi-Pi stacking\u003c/strong\u003e at HIS A:322 further supports the aromatic stabilization of the complex. The presence of\u0026nbsp;\u003cstrong\u003eunfavorable donor-donor\u003c/strong\u003e interactions at ASN A:325, similar to what was observed with Isoliquiritin, again points to areas where ligand optimization could potentially improve the binding efficiency or reduce instability.\u003c/p\u003e\n\u003cp\u003eOverall, the data reveals a mix of favorable and unfavorable interactions, with hydrophobic and aromatic interactions playing prominent roles in stabilizing the binding of the licorice-derived compounds to the ZYMV-P3 protein. The presence of unfavorable interactions in some cases suggests areas for potential optimization in the ligand structure. These insights into protein-ligand binding dynamics may contribute to the development of more effective antiviral strategies targeting ZYMV-P3.\u003c/p\u003e\n\u003cp\u003eThe results in Table 5 \u0026amp; Fig. 4 presented outlines the specific bonding interactions between four licorice-derived bioactive compounds\u0026mdash;Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin\u0026mdash;and the ZYMV-6K1 protein. These interactions help to identify how each compound binds to specific amino acid residues of the protein, which could provide insights into their potential biological activities or roles in therapeutic applications, particularly in relation to ZYMV (Zucchini yellow mosaic virus) infection.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic acid forms a variety of bonding interactions with the ZYMV-6K1 protein. For example, the amino acid phenylalanine (PHE) at position A:23 forms an alkyl bond with Glycyrrhetic acid, indicating a hydrophobic interaction. Additionally, the interaction between IsoLeucine (ILE) at A:34 and Glycyrrhetic acid is more complex, involving alkyl, Pi-Alkyl, and conventional hydrogen bonds, suggesting a multifaceted mode of interaction that likely stabilizes the binding. Phenylalanine at A:32 also interacts via Pi-Alkyl bonding, highlighting its role in the aromatic \u0026pi;-\u0026pi; interactions that may contribute to the stability of the complex.\u003c/p\u003e\n\u003cp\u003eIsoliquiritin interacts with ZYMV-6K1 through conventional hydrogen bonds with aspartic acid (ASP) at A:24 and arginine (ARG) at A:27, which are typical of electrostatic interactions. These hydrogen bonds can play a role in enhancing the binding specificity between the compound and the protein. The interaction of phenylalanine (PHE) at A:23 via Pi-Pi T-Shaped bonding indicates \u0026pi;-\u0026pi; stacking interactions, which are often seen in ligand-receptor binding where aromatic rings play a key role. IsoLeucine (ILE) at A:34 forms a Pi-Sigma bond with isoliquiritin, indicating another level of interaction between the compound and the protein\u0026apos;s hydrophobic regions.\u003c/p\u003e\n\u003cp\u003eLiquiritin also forms hydrogen bonds with ARG (A:27), similar to isoliquiritin, but it also exhibits an unfavorable donor-donor interaction with lysine (LYS) at A:37. This unfavorable interaction suggests that the binding of liquiritin might not be as stable in this region, potentially leading to a weaker or less specific binding at this site. As with the other compounds, phenylalanine (PHE) at A:23 forms a Pi-Pi T-Shaped interaction, contributing to a strong, stabilizing aromatic interaction. Additionally, ILE at A:34 forms Pi-Sigma interactions, further suggesting that the hydrophobic binding pocket of ZYMV-6K1 plays an essential role in binding liquiritin.\u003c/p\u003e\n\u003cp\u003eGlabridin exhibits a complex pattern of bonding with ZYMV-6K1, with multiple interactions seen in the table. IsoLeucine (ILE) at A:34 forms a Pi-Sigma interaction, a common feature across several of the bioactive compounds, emphasizing the importance of hydrophobic interactions in these complexes. Valine (VAL) at A:41 engages in Pi-Alkyl bonding, reinforcing the importance of hydrophobic regions in stabilizing glabridin binding. Leucine (LEU) at A:38 forms Pi-Alkyl interactions, which could be involved in stabilizing the binding pocket. Interestingly, lysine (LYS) at A:37 is involved in multiple types of bonding, including Alkyl and Pi-Alkyl interactions, as well as a Pi-Cation bond. This suggests that lysine may play a critical role in facilitating strong, multifaceted binding with glabridin. Additionally, Leucine at A:16 forms multiple Pi-Alkyl and Alkyl interactions, contributing to the overall stability of the protein-ligand complex.\u003c/p\u003e\n\u003cp\u003eIn a conclusion, the interactions detailed in the table underscore the importance of both hydrophobic (alkyl, Pi-Alkyl) and electrostatic (hydrogen bonds) forces in mediating the binding of licorice-derived compounds to ZYMV-6K1. These interactions can provide insights into the structural dynamics of protein-ligand binding and may help guide the design of more effective bioactive molecules for therapeutic applications against ZYMV or other related viruses. The varied types of bonds also highlight the versatility of these compounds in recognizing and stabilizing interactions with different amino acid residues, which is critical for their potential efficacy.\u003c/p\u003e\n\u003cp\u003eResults in Table 6 \u0026amp; Fig. 5 showed that the bonding interactions between four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-CI protein reveal a complex network of interactions that could help elucidate the binding dynamics of these compounds with the protein.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic acid interacts with several amino acids in ZYMV-CI, exhibiting Pi-Alkyl interactions with Proline (PRO) at positions A:207 and A:378, which are indicative of hydrophobic bonding. These interactions suggest a strong hydrophobic interface that may contribute to the stability of the binding. Additionally, threonine (THR) at A:179 and serine (SER) at A:376 form carbon-hydrogen bonds with the compound, implying weaker, but still significant, electrostatic interactions. Proline at A:378 also forms multiple Pi-Alkyl bonds, further emphasizing the role of hydrophobic regions in stabilizing the complex. Histidine (HIS) at A:177 and threonine (THR) at A:205 participate in carbon-hydrogen and Pi-Donor-H bonds, respectively, suggesting that these residues play a supportive role in binding through weaker hydrogen bonds and donor interactions.\u003c/p\u003e\n\u003cp\u003eIsoliquiritin, similar to Glycyrrhetic acid, interacts with threonine (THR) at A:205 through a Pi-Donor-H bond, which may facilitate the ligand\u0026apos;s positioning within the protein\u0026rsquo;s binding pocket. Proline (PRO) at A:207 forms a Pi-Alkyl interaction, reinforcing hydrophobic binding. Isoliquiritin also establishes conventional hydrogen bonds with serine (SER) at A:376, and more importantly, it forms unfavorable donor-donor interactions with arginine (ARG) at A:209 and asparagine (ASN) at A:187. These unfavorable interactions may suggest less optimal binding or potential destabilization in certain regions. The conventional hydrogen bonds with ASN at A:187 further complicate the interaction profile, revealing possible competition or steric hindrance at this binding site.\u003c/p\u003e\n\u003cp\u003eLiquiritin shares several interactions with isoliquiritin, including Pi-Alkyl interactions with Proline (PRO) at A:207 and Pi-Donor-H interactions with threonine (THR) at A:205. Glycine (GLY) at A:208 forms both conventional hydrogen bonds and Pi-Donor-H bonds with the compound, which may help anchor the compound within the protein. However, like isoliquiritin, liquiritin also exhibits unfavorable donor-donor interactions with asparagine (ASN) at A:310 and A:187. These unfavorable interactions again suggest potential instability or weak binding at these sites, possibly reducing the overall binding affinity in these regions.\u003c/p\u003e\n\u003cp\u003eGlabridin\u0026rsquo;s interactions with ZYMV-CI are marked by several key features. Proline (PRO) at A:207 forms alkyl bonds, which are likely to contribute to hydrophobic interactions. Similar to other compounds, glabridin interacts with threonine (THR) at A:179 and serine (SER) at A:376 through Pi-Donor-H bonds, indicating a preference for donor-acceptor interactions in these regions. Proline at A:378 also forms multiple Pi-Alkyl bonds, as well as a Pi-Sigma bond, suggesting a particularly strong hydrophobic interaction at this site. The compound\u0026apos;s interactions with Histidine (HIS) at A:177 and threonine (THR) at A:205 through carbon-hydrogen and Pi-Donor-H bonds demonstrate the importance of both hydrogen and donor interactions in the overall binding of glabridin.\u003c/p\u003e\n\u003cp\u003eIn summary, the interactions between the licorice-derived bioactive compounds and ZYMV-CI indicate a mixture of hydrophobic, hydrogen bonding, and donor-acceptor interactions. The hydrophobic interactions, especially with Proline and threonine, seem to play a major role in stabilizing the compounds within the protein. At the same time, the presence of unfavorable donor-donor interactions in some cases suggests that the binding may not be perfectly optimized, potentially reducing the affinity or stability of the ligand-protein complex at certain sites. These findings provide insights into how these compounds may interact with ZYMV-CI and could be useful for designing more effective therapeutics targeting this protein.\u003c/p\u003e\n\u003cp\u003eResults in Table 7 \u0026amp; Fig. 6 detailing the bonding interactions between four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-6K2 protein provides valuable insights into the nature of these interactions, which could influence the binding affinity and stability of the protein-ligand complexes.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic acid interacts primarily with tryptophan (TRP) at position D:36 through multiple Pi-Alkyl bonds. These interactions, characteristic of hydrophobic regions, suggest that tryptophan\u0026rsquo;s aromatic ring plays a significant role in stabilizing the binding of Glycyrrhetic acid. The multiple Pi-Alkyl interactions likely contribute to the overall strength and specificity of this binding site, with tryptophan acting as a key residue in the protein-ligand interaction.\u003c/p\u003e\n\u003cp\u003eIsoliquiritin binds with ZYMV-6K2 through a variety of interactions. Asparagine (ASN) at D:22 forms conventional hydrogen bonds with the compound, while also displaying an unfavorable donor-donor interaction, which could reduce the overall binding efficiency or stability at this site. The interaction of tryptophan (TRP) at D:15 with isoliquiritin involves Pi-Pi stacked bonding, which is indicative of aromatic stacking interactions that contribute to the stability of the complex. Lysine (LYS) at D:19 participates in Pi-Alkyl interactions, highlighting its role in stabilizing the hydrophobic portion of the ligand. Aspartic acid (ASP) at D:23 interacts through Pi-Anion bonding, as well as conventional hydrogen bonds, and also displays an unfavorable donor-donor interaction, suggesting potential areas of weaker or less optimal binding.\u003c/p\u003e\n\u003cp\u003eLiquiritin engages with ZYMV-6K2 through van der Waals forces with glycine (GLY) at D:33, which are typically weak but can help to fine-tune the overall binding interaction. Methionine (MET) at D:29 forms Pi-Alkyl interactions, contributing to the hydrophobic stabilization of the ligand in the binding pocket. Additionally, Leucine (LEU) at D:32 forms amide-Pi stacked interactions, which suggest that the compound may benefit from multiple levels of stabilization through both hydrophobic and potential hydrogen bonding interactions, further enhancing the overall stability of the complex.\u003c/p\u003e\n\u003cp\u003eGlabridin interacts with ZYMV-6K2 through several key residues. Lysine (LYS) at D:19 forms both Pi-Alkyl and alkyl bonds with the compound, indicating that its hydrophobic side chains contribute to stabilizing the binding site. Tryptophan (TRP) at D:15 shows an even more intricate pattern of interactions, with Pi-Alkyl, alkyl, and Pi-Pi stacked bonds. These multiple interactions, particularly the Pi-Pi stacking, suggest that tryptophan plays a central role in the binding of glabridin, likely stabilizing the complex through aromatic interactions.\u003c/p\u003e\n\u003cp\u003eIn summary, the bonding interactions between the licorice-derived compounds and ZYMV-6K2 highlight a combination of hydrophobic (Pi-Alkyl, Pi-Pi stacked), electrostatic (conventional hydrogen bonds, Pi-Anion), and weak van der Waals interactions. These interactions indicate that hydrophobic regions, particularly involving tryptophan, lysine, and methionine, play a critical role in stabilizing the binding of the compounds to the protein. However, the presence of unfavorable donor-donor interactions in some cases, such as with asparagine and aspartic acid, may suggest areas where the binding is less stable or efficient, potentially limiting the overall effectiveness of these compounds in modulating ZYMV-6K2 activity.\u003c/p\u003e\n\u003cp\u003eResults in Table 8 \u0026amp; Fig. 7 demonstrated that the interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-NIa-VPg protein provide a detailed look at how these compounds bind to various amino acid residues, potentially influencing the protein\u0026apos;s function and stability.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic acid binds with several amino acids in ZYMV-NIa-VPg, primarily through hydrophobic interactions. Proline (PRO) at position A:143 forms carbon-hydrogen and alkyl bonds, indicating that the compound interacts with the hydrophobic regions of the protein. Similarly, Valine (VAL) at A:96 and IsoLeucine (ILE) at A:93 form alkyl interactions, which help anchor the compound within the protein\u0026apos;s binding pocket. IsoLeucine at A:124 and Leucine (LEU) at A:141 also contribute to the binding with alkyl interactions, further stabilizing the compound through hydrophobic forces. These interactions suggest that the binding of Glycyrrhetic acid to ZYMV-NIa-VPg is largely driven by hydrophobic interactions, which are critical for stabilizing the ligand within the protein.\u003c/p\u003e\n\u003cp\u003eIsoliquiritin interacts with ZYMV-NIa-VPg through a variety of bonding mechanisms. Aspartic acid (ASP) at A:78 forms conventional hydrogen bonds with isoliquiritin, enhancing its stability in the binding pocket. Threonine (THR) at A:91, however, exhibits an unfavorable acceptor-acceptor interaction, suggesting that this particular binding site might not be optimal for isoliquiritin, possibly reducing its overall binding affinity. Threonine at A:89 forms conventional hydrogen bonds, further stabilizing the interaction. IsoLeucine (ILE) at A:124 interacts via Pi-Sigma and Pi-Alkyl bonding, indicating the presence of both aromatic and hydrophobic interactions that contribute to the overall binding strength.\u003c/p\u003e\n\u003cp\u003eLiquiritin binds to ZYMV-NIa-VPg through several hydrophobic interactions, as well as hydrogen bonding. Lysine (LYS) at A:121 forms conventional hydrogen bonds, suggesting some electrostatic contribution to the binding. Aspartic acid (ASP) at A:78 also forms conventional hydrogen bonds, further contributing to the stabilization of the ligand-protein complex. Leucine (LEU) at A:141 forms Pi-Sigma interactions, likely stabilizing the complex through aromatic interactions. IsoLeucine (ILE) at A:124 participates in Pi-Sigma bonding, contributing to the overall stability of the interaction. Additionally, Valine (VAL) at A:96 and IsoLeucine (ILE) at A:93 form Pi-Alkyl bonds, which further stabilize the binding through hydrophobic interactions, suggesting that the ligand binds primarily through non-polar forces.\u003c/p\u003e\n\u003cp\u003eGlabridin shows a similar interaction profile to the other compounds, with multiple hydrophobic interactions that contribute to the binding stability. Leucine (LEU) at A:141 forms Pi-Alkyl bonds, stabilizing the complex through hydrophobic interactions. IsoLeucine (ILE) at A:124 engages in a complex set of interactions, including alkyl, Pi-Alkyl, Pi-Alkyl, and Pi-Sigma bonds. These multiple types of bonding suggest that IsoLeucine at this site plays a critical role in stabilizing glabridin binding through a combination of hydrophobic and aromatic interactions. IsoLeucine at A:93 also forms alkyl, Pi-Alkyl, and Pi-Sigma bonds, further reinforcing the binding of glabridin to the protein. Finally, Valine (VAL) at A:96 contributes to the binding through Pi-Alkyl interactions, stabilizing the hydrophobic regions of the protein-ligand complex.\u003c/p\u003e\n\u003cp\u003eIn summary, the bonding interactions between these licorice-derived compounds and the ZYMV-NIa-VPg protein are dominated by hydrophobic interactions, particularly those involving alkyl, Pi-Alkyl, and Pi-Sigma bonds. These interactions are critical for stabilizing the binding of the compounds within the protein\u0026apos;s hydrophobic pockets. Additionally, the presence of conventional hydrogen bonds, as seen with aspartic acid and lysine, suggests that electrostatic interactions also play a role in stabilizing the complexes. The unfavorable acceptor-acceptor interactions observed with isoliquiritin indicate that not all binding sites are equally favorable for these compounds, which may affect the overall binding affinity and specificity. These findings suggest that the ligands interact primarily through non-polar forces, with some contributions from hydrogen bonding, making the protein-ligand interactions potentially more dynamic and adaptable for therapeutic targeting.\u003c/p\u003e\n\u003cp\u003eThe bonding interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-NIa-Pro protein (Table 9 \u0026amp; Fig. 8) demonstrate a range of hydrophobic and electrostatic interactions that likely influence the binding efficiency and stability of the complexes.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic acid interacts with several key amino acids in ZYMV-NIa-Pro, with a primary focus on hydrophobic interactions. Lysine (LYS) at A:6 and tyrosine (TYR) at A:11 form conventional hydrogen bonds, indicating that these residues contribute to the electrostatic stabilization of the compound within the protein. Valine (VAL) at A:125 interacts through alkyl bonds, which stabilize the ligand through hydrophobic interactions. Tyrosine at A:5 contributes to the binding with a Pi-Alkyl interaction, suggesting that the aromatic ring of tyrosine is involved in stabilizing the interaction through \u0026pi;-\u0026pi; interactions. These hydrophobic interactions, along with conventional hydrogen bonds, suggest that Glycyrrhetic acid binds primarily through both electrostatic and hydrophobic forces.\u003c/p\u003e\n\u003cp\u003eIsoliquiritin binds with ZYMV-NIa-Pro through a combination of conventional hydrogen bonds and aromatic interactions. Alanine (ALA) at A:170 forms Pi-Sigma and conventional hydrogen bonds with the compound, stabilizing the interaction through both electrostatic and \u0026pi;-\u0026pi; interactions. Glycine (GLY) at A:168 also forms conventional hydrogen bonds, further contributing to the stabilization of the complex. However, lysine (LYS) at A:29 exhibits an unfavorable acceptor-acceptor interaction, indicating that this particular region may not be optimal for binding, potentially reducing the stability of the complex at this site. Threonine (THR) at A:146 contributes to the binding through conventional hydrogen bonds, supporting the overall stability of the ligand within the protein.\u003c/p\u003e\n\u003cp\u003eLiquiritin exhibits multiple interactions with ZYMV-NIa-Pro, including both hydrophobic and electrostatic bonding. Glutamic acid (GLU) at A:220 and A:30 forms unfavorable acceptor-acceptor interactions and conventional hydrogen bonds, respectively. The unfavorable interaction at A:220 suggests a less favorable binding region, while the conventional hydrogen bond at A:30 helps stabilize the binding. Alanine (ALA) at A:170 forms Pi-Alkyl interactions, contributing to the hydrophobic stabilization of the ligand. Cysteine (CYS) at A:151 forms Pi-Alkyl bonds, further stabilizing the complex through hydrophobic interactions. Asparagine (ASN) at A:147 and threonine (THR) at A:146 contribute conventional hydrogen bonds, further enhancing the overall binding affinity. Glutamine (GLN) at A:221 also forms a conventional hydrogen bond, supporting the electrostatic stabilization of the ligand.\u003c/p\u003e\n\u003cp\u003eGlabridin interacts with ZYMV-NIa-Pro through specific hydrophobic and electrostatic interactions. Glutamic acid (GLU) at A:148 forms Pi-Anion bonds with the compound, stabilizing the interaction through electrostatic forces. Alanine (ALA) at A:170 forms Pi-Alkyl bonds, contributing to the hydrophobic interaction. These interactions suggest that Glabridin binds primarily through hydrophobic and electrostatic forces, with glutamic acid and alanine playing key roles in stabilizing the complex.\u003c/p\u003e\n\u003cp\u003eIn summary, the bonding interactions of the licorice-derived compounds with ZYMV-NIa-Pro are characterized by a mix of hydrophobic interactions (such as alkyl, Pi-Alkyl, and Pi-Sigma) and electrostatic interactions (including conventional hydrogen and Pi-Anion bonds). These interactions collectively contribute to the stability and specificity of the complexes. However, the presence of unfavorable donor-acceptor interactions, such as those with lysine in Isoliquiritin and glutamic acid in Liquiritin, suggests that some regions of the binding sites are less optimal for certain compounds, which may reduce the overall binding strength or efficiency. Nonetheless, these findings provide important insights into the potential for these bioactive compounds to modulate the activity of ZYMV-NIa-Pro.\u003c/p\u003e\n\u003cp\u003eThe bonding interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-NIb protein (Table 10 \u0026amp; Fig. 9) reveal a complex set of interactions, highlighting both hydrophobic and electrostatic forces, which likely contribute to the stability and specificity of the binding.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid\u003c/strong\u003e shows strong hydrophobic interactions with several amino acids in ZYMV-NIb, primarily through alkyl and Pi-Alkyl interactions. Leucine (LEU) at positions A:122, A:152, and A:198, along with Valine (VAL) at A:202 and methionine (MET) at A:281, contribute alkyl bonds, stabilizing the compound through hydrophobic interactions. Tyrosine (TYR) at A:119 interacts via Pi-Sigma bonding, further reinforcing the stability of the complex through aromatic interactions. Phenylalanine (PHE) at A:140 also participates in Pi-Alkyl bonds, highlighting the importance of aromatic and hydrophobic interactions in stabilizing Glycyrrhetic acid within the binding pocket. However, arginine (ARG) at A:148 forms an unfavorable donor-donor interaction, indicating that this site might not contribute optimally to the binding, potentially destabilizing the interaction at this location. Serine (SER) at A:121 and cysteine (CYS) at A:203 form conventional hydrogen bonds, further contributing to the stabilization of Glycyrrhetic acid in the protein\u0026apos;s binding site. Lysine (LYS) at A:135 also participates in a conventional hydrogen bond, adding to the overall electrostatic stabilization of the complex.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eIsoliquiritin\u003c/strong\u003e interacts with ZYMV-NIb through a combination of Pi-Sigma, conventional hydrogen, and hydrophobic bonds. Threonine (THR) at A:81 forms Pi-Sigma bonds with the compound, stabilizing the interaction through aromatic interaction. Asparagine (ASN) at A:184 contributes conventional hydrogen bonds, as does aspartic acid (ASP) at A:253 and A:352, providing additional electrostatic stabilization. However, the serine (SER) at A:254 forms an unfavorable donor-donor interaction, which may reduce the stability of the binding at this site. Arginine (ARG) at A:187 forms Pi-Alkyl and conventional hydrogen bonds, contributing both hydrophobic and electrostatic forces to the binding, while lysine (LYS) at A:185 stabilizes the complex through Pi-Alkyl interactions.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eLiquiritin\u003c/strong\u003e shows a broad range of interactions, with both hydrophobic and electrostatic components. Glutamic acid (GLU) at A:116 and IsoLeucine (ILE) at A:118 form carbon-hydrogen bonds, contributing weaker interactions that may help position the compound in the binding pocket. Serine (SER) at A:121 forms conventional hydrogen bonds, stabilizing the binding. Leucine (LEU) at A:198 participates in Pi-Sigma bonding, enhancing the hydrophobic stabilization of the complex. Tyrosine (TYR) at A:119 forms a Pi-Pi T-shaped interaction, indicative of aromatic stacking, which likely helps in stabilizing the ligand. Valine (VAL) at A:202 forms Pi-Alkyl bonds, further stabilizing the interaction through hydrophobic forces. Aspartic acid (ASP) at A:205 and A:206 contribute conventional hydrogen bonds, while phenylalanine (PHE) at A:207 participates in both conventional hydrogen bonding and carbon-hydrogen bonding, offering both electrostatic and hydrophobic stabilization to the complex.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eGlabridin\u003c/strong\u003e interacts with ZYMV-NIb primarily through alkyl and conventional hydrogen bonds. Serine (SER) at A:310 forms a conventional hydrogen bond, helping to stabilize the ligand within the binding pocket. Arginine (ARG) at A:187 and lysine (LYS) at A:185 form alkyl bonds, contributing hydrophobic stabilization, while lysine at A:304 forms a conventional hydrogen bond, further stabilizing the binding. The presence of alkyl interactions in key positions suggests that the binding of Glabridin is largely driven by hydrophobic forces, with some additional electrostatic contributions from the hydrogen bonds.\u003c/p\u003e\n\u003cp\u003eIn summary, the interactions between the licorice-derived bioactive compounds and ZYMV-NIb are dominated by hydrophobic interactions, particularly those involving alkyl, Pi-Alkyl, Pi-Sigma, and Pi-Pi bonds. These interactions suggest that the compounds primarily interact with hydrophobic regions of the protein, stabilizing the complexes within the binding site. Additionally, conventional hydrogen bonds and some unfavorable donor-donor interactions contribute to the overall binding stability. The presence of unfavorable interactions, such as those with serine in Isoliquiritin and glutamic acid in Liquiritin, may indicate regions of suboptimal binding, which could reduce the overall binding efficiency of the complexes. Nonetheless, these findings highlight the significant role of hydrophobic interactions in the binding of licorice-derived compounds to ZYMV-NIb, suggesting that these compounds may serve as potential modulators of protein function through their binding dynamics.\u003c/p\u003e\n\u003cp\u003eThe bonding interactions between the four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-and the ZYMV-CP protein (Table 11 \u0026amp; Fig. 10) reflect a range of interactions, with hydrophobic forces and electrostatic bonds playing significant roles in stabilizing the binding of these compounds to the protein.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid\u003c/strong\u003e primarily forms hydrophobic interactions with several amino acids in ZYMV-CP, with alkyl and Pi-Alkyl interactions at key positions. Alanine (ALA) at B:39 engages in both alkyl and Pi-Alkyl bonds, which help anchor the compound within the protein\u0026rsquo;s hydrophobic pocket. Lysine (LYS) at C:44 forms conventional hydrogen bonds, contributing to the electrostatic stabilization of the complex. Phenylalanine (PHE) at C:36 and lysine (LYS) at C:34 contribute alkyl interactions, further stabilizing the binding through hydrophobic forces. These interactions suggest that Glycyrrhetic acid binds primarily through hydrophobic forces, with some additional electrostatic stabilization provided by conventional hydrogen bonds.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eIsoliquiritin\u003c/strong\u003e interacts with ZYMV-CP through a combination of hydrophobic and electrostatic bonds. Lysine (LYS) at C:41 forms Pi-Alkyl bonds, indicating the presence of both hydrophobic and \u0026pi;-\u0026pi; interactions that contribute to stabilizing the ligand in the protein\u0026apos;s binding pocket. Proline (PRO) at C:38 forms conventional hydrogen bonds, adding to the electrostatic stabilization. However, arginine (ARG) at C:42 forms an unfavorable donor-donor interaction, which could reduce the overall binding strength at this site. Lysine (LYS) at C:44 forms a more favorable combination of Pi-Alkyl, conventional hydrogen, and Pi-Anion interactions, contributing significantly to the stability of the complex. Aspartic acid (ASP) at C:30 forms a Pi-Cation interaction, suggesting that electrostatic interactions also play a role in stabilizing the binding. Additionally, Leucine (LEU) at C:29 engages in Pi-Sigma bonding, which further strengthens the hydrophobic component of the binding.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eLiquiritin\u003c/strong\u003e shows a variety of bonding types with ZYMV-CP, including both hydrophobic and electrostatic interactions. Arginine (ARG) at C:23 forms unfavorable donor-donor interactions along with conventional hydrogen bonds, indicating that the binding at this site may not be ideal. Asparagine (ASN) at B:37 and phenylalanine (PHE) at C:31 both form conventional hydrogen bonds, helping stabilize the ligand in the protein. Alanine (ALA) at B:39 forms Pi-Alkyl bonds, contributing to the hydrophobic stabilization of the complex. Arginine (ARG) at B:42 forms a conventional hydrogen bond, further supporting the electrostatic stabilization of the binding. Glutamic acid (GLU) at C:26 forms multiple conventional hydrogen bonds and carbon-hydrogen interactions, contributing to both electrostatic and hydrophobic stabilization of the ligand.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eGlabridin\u003c/strong\u003e interacts with ZYMV-CP through a combination of hydrophobic and electrostatic forces. Alanine (ALA) at A:39 forms both Pi-Sigma and alkyl bonds, suggesting that this site is crucial for stabilizing the compound through both hydrophobic and aromatic interactions. Aspartic acid (ASP) at B:30 forms conventional hydrogen and Pi-Cation bonds, which stabilize the complex through electrostatic interactions. Arginine (ARG) at A:42 forms a Pi-Anion bond, indicating a significant contribution of electrostatic forces to the binding. Alanine (ALA) at B:27 forms Pi-Alkyl bonds, further contributing to the hydrophobic stabilization of the ligand. Proline (PRO) at A:38 also forms Pi-Alkyl bonds, supporting the hydrophobic nature of the binding.\u003c/p\u003e\n\u003cp\u003eIn summary, the bonding interactions between the licorice-derived bioactive compounds and ZYMV-CP are characterized by a blend of hydrophobic and electrostatic forces. The majority of interactions involve alkyl, Pi-Alkyl, Pi-Sigma, and Pi-Anion bonds, highlighting the importance of hydrophobic interactions in stabilizing these complexes. Conventional hydrogen bonds contribute further to the electrostatic stabilization of the protein-ligand interactions. However, the presence of unfavorable donor-donor interactions, as seen with arginine in Isoliquiritin and Liquiritin, and glutamic acid in Liquiritin, suggests that some regions of the binding sites may not be optimal for these compounds, potentially reducing their overall binding affinity. Despite this, the predominance of hydrophobic interactions suggests that these compounds primarily stabilize their binding to ZYMV-CP through non-polar interactions, which could be critical for modulating the protein\u0026apos;s function or activity.\u003c/p\u003e"},{"header":"Discussion","content":"\u003cp\u003eRegarding ZTMV-P1 protein the data highlighted various bonding interactions between licorice-derived bioactive compounds and the ZYMV-P1 protein, including hydrogen bonds, alkyl interactions, Pi-Alkyl, and Pi-based interactions. These interactions play a crucial role in stabilizing the protein-ligand complex, particularly hydrogen bonds, which contribute significantly to the binding affinity and specificity of the compounds. This is consistent with previous studies indicating the importance of hydrogen bonding in protein-ligand recognition and stability [22, 23].\u003c/p\u003e\n\u003cp\u003eHydrophobic interactions, including alkyl and Pi-Alkyl interactions, also contribute to stabilizing the binding of non-polar ligands. These interactions are critical for the binding of larger ligands and enhance stability through aromatic stacking [24]. The prevalence of these interactions suggests that licorice compounds likely use hydrophobic and aromatic forces to interact with the ZYMV-P1 protein, contributing to their antiviral potential.\u003c/p\u003e\n\u003cp\u003eThe analysis also identifies unfavorable donor-donor and acceptor-acceptor interactions, which are energetically less favorable and can cause steric clashes. These interactions highlight areas for ligand optimization, as modifying functional groups to avoid such clashes could enhance binding affinity and specificity [25]. Addressing these unfavorable interactions could improve the potency of these compounds as antiviral agents [26].\u003c/p\u003e\n\u003cp\u003eThese findings suggest that licorice-derived compounds like glycyrrhizin could serve as a promising foundation for antiviral drug development. By optimizing their interactions with viral proteins and reducing unfavorable interactions, researchers can design more effective inhibitors targeting ZYMV and related viruses. Natural compounds like those derived from licorice offer a potential alternative to synthetic drugs, providing safer and more targeted antiviral therapies [27].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eThe interactions between the ZYMV-HC-Pro protein and four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-demonstrate a complex range of bonding types, including conventional hydrogen bonds, hydrophobic alkyl interactions, pi-stacking interactions, and specialized Pi-Anion and Pi-Sulfur bonds. These findings indicate the multifaceted nature of protein-ligand binding and the potential of these compounds as inhibitors of ZYMV-HC-Pro.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic Acid interactions are primarily dominated by hydrophobic alkyl bonds with residues like CYS A:342 and ALA A:337. Hydrogen bonds at TYR A:335 further stabilize the binding, suggesting a highly favorable binding environment [28].\u003c/p\u003e\n\u003cp\u003eIsoliquiritin shows significant aromatic interactions, including Pi-Alkyl interactions at VAL A:352 and Pi-Anion interactions at GLU A:401, which contribute to its binding stability [24]. The diversity of bonding types at GLU A:401 indicates a complex and specific binding mode. Liquiritin engages in both hydrogen bonding and Pi-Sulfur interactions, the latter being important for enzyme-inhibitor complexes [29]. However, an unfavorable donor-donor interaction at HIS A:415 suggests opportunities for ligand optimization [26]. Glabridin interacts through a combination of conventional hydrogen bonds and specialized Pi-Anion bonds at GLU A:401 and ASP A:418, along with hydrophobic interactions like Pi-Alkyl at ALA A:349. These interactions indicate a strong binding affinity driven by both electrostatic and hydrophobic forces [28].\u003c/p\u003e\n\u003cp\u003eThe interactions between the ZYMV-P3 protein and four licorice-derived bioactive compounds-Glycyrrhetic acid, Isoliquiritin, Liquiritin, and Glabridin-reveal a range of hydrophobic, aromatic, and polar interactions, all contributing to binding stability and specificity.\u003c/p\u003e\n\u003cp\u003eGlycyrrhetic Acid demonstrates hydrophobic alkyl bonds at ILE A:305 and HIS A:322, which stabilize the ligand within a non-polar binding pocket. Pi-Alkyl and Pi-Sigma interactions further reinforce the binding, while conventional hydrogen bonds at SER A:307 enhance the overall affinity [28, 24]. This combination of interactions suggests a stable, energetically favorable complex.\u003c/p\u003e\n\u003cp\u003eIsoliquiritin exhibits some unfavorable donor-donor interactions at ARG A:327 and ASN A:325, indicating areas for optimization [26]. However, it also maintains stabilizing Pi-Sigma and Pi-Pi stacking interactions at ILE A:305 and HIS A:322, contributing to overall binding stability. A conventional hydrogen bond at ASP A:329 also enhances the interaction. Liquiritin shares similar interactions with Isoliquiritin, with key Pi-Pi stacking and Pi-Alkyl interactions at HIS A:322 and ILE A:305. Conventional hydrogen bonds further stabilize the binding, although unfavorable donor-donor interactions at ASN A:325 suggest optimization opportunities. Glabridin has a more complex interaction profile, with strong hydrophobic and Pi-Anion interactions at ARG A:327, ILE A:305, and ASP A:329, contributing to overall stability. Pi-Pi stacking interactions at HIS A:322 also play a role. However, it shares the unfavorable donor-donor interactions seen in Isoliquiritin, indicating areas for improvement in the ligand structure.\u003c/p\u003e\n\u003cp\u003eThe analysis of the bonding interactions between licorice-derived bioactive compounds and the ZYMV-CI protein reveals the importance of hydrophobic, electrostatic, and donor-acceptor interactions in stabilizing the ligand-protein complex. Glycyrrhetic acid shows strong Pi-Alkyl interactions, particularly with Proline residues, and weaker electrostatic contributions, suggesting a balanced binding profile [24]. Isoliquiritin and Liquiritin share similar profiles but exhibit unfavorable donor-donor interactions with asparagine and arginine, potentially destabilizing the complex in these regions [26]. These steric clashes or electrostatic repulsions highlight areas for optimization to improve binding affinity.\u003c/p\u003e\n\u003cp\u003eGlabridin, like the other compounds, demonstrates hydrophobic interactions (Pi-Alkyl) with Proline and additional donor-acceptor bonds, further stabilizing the complex [26]. These interactions collectively emphasize the crucial role of hydrophobic regions, especially the Pi-Alkyl bonds, in stabilizing the complexes, while electrostatic interactions help enhance specificity and binding strength.\u003c/p\u003e\n\u003cp\u003eThe analysis of bonding interactions between licorice-derived bioactive compounds and the ZYMV-6K2 protein reveals key insights into the stability and specificity of the protein-ligand complex. Glycyrrhetic acid forms strong Pi-Alkyl interactions with tryptophan (TRP) residues, which play a pivotal role in stabilizing the binding, underlining the importance of hydrophobic interactions in protein-ligand binding [24].\u003c/p\u003e\n\u003cp\u003eIsoliquiritin shares similar hydrophobic interactions but also exhibits unfavorable donor-donor interactions with asparagine (ASN), suggesting areas for improvement in binding efficiency [26]. Additionally, it demonstrates aromatic interactions with TRP and hydrophobic contributions from lysine (LYS) residues, which enhance the stability of the complex [24]. Liquiritin also interacts with hydrophobic residues like methionine (MET) and Leucine (LEU) through Pi-Alkyl and amide-Pi stacking interactions. However, it similarly presents unfavorable donor-donor interactions with ASN residues, which could reduce binding stability [26]. Glabridin, like the other compounds, benefits from hydrophobic interactions with TRP and LYS residues, with Pi-Pi stacking providing additional stability. However, unfavorable donor-donor interactions with ASN residues highlight areas for optimization [24].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eThe bonding interactions between the four licorice-derived bioactive compounds and the ZYMV-NIa-VPg protein reveal that hydrophobic interactions are the primary stabilizing force, with hydrogen bonding also contributing to the overall binding stability. Glycyrrhetic acid primarily forms hydrophobic interactions, particularly with Proline (PRO), Valine (VAL), and IsoLeucine (ILE), highlighting the importance of non-polar forces in stabilizing the complex [28]. These hydrophobic interactions suggest the ligand fits well into the protein\u0026apos;s hydrophobic pocket, reinforcing its stability [24]. Isoliquiritin engages in both hydrophobic and electrostatic interactions, with hydrogen bonds formed with aspartic acid (ASP) and threonine (THR). However, unfavorable acceptor-acceptor interactions at THR suggest areas where optimization could improve binding efficiency [26]. The presence of both aromatic and hydrophobic interactions indicates a combination of forces that stabilize the ligand-protein complex [28].\u003c/p\u003e\n\u003cp\u003eLiquiritin\u0026rsquo;s binding is similarly dominated by hydrophobic interactions, particularly with residues like Leucine (LEU), IsoLeucine (ILE), and Valine (VAL), which form Pi-Sigma, Pi-Alkyl, and alkyl bonds. Additionally, hydrogen bonds with aspartic acid (ASP) and lysine (LYS) further stabilize the complex [24]. These interactions emphasize the role of hydrophobic forces in stabilizing the complex [24].\u003c/p\u003e\n\u003cp\u003eGlabridin also shows a similar profile, with hydrophobic interactions formed with IsoLeucine (ILE) and Leucine (LEU). These interactions, along with multiple types of bonds, suggest that hydrophobic forces dominate the binding process, contributing to the overall stability of the complex [28].\u003c/p\u003e\n\u003cp\u003eThe results highlight the critical role of hydrophobic interactions, particularly alkyl, Pi-Alkyl, and Pi-Sigma bonds, in stabilizing these licorice-derived compounds within the ZYMV-NIa-VPg binding pocket. While electrostatic interactions also contribute, the presence of unfavorable interactions, especially with certain residues like threonine, suggests areas where ligand optimization could improve binding affinity and stability [26]. These findings offer valuable insights into developing more effective therapeutic agents targeting ZYMV.\u003c/p\u003e\n\u003cp\u003eThe interactions between the four licorice-derived bioactive compounds and the ZYMV-NIa-Pro protein involve both hydrophobic and electrostatic forces, affecting binding stability and specificity. Glycyrrhetic Acid\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003ePrimarily forms hydrophobic (alkyl, Pi-Alkyl) interactions with Valine and Tyrosine, alongside electrostatic hydrogen bonds with Lysine and Tyrosine, stabilizing the complex [28]. Isoliquiritin, forms both hydrogen bonds and aromatic interactions. However, the Lysine residue creates an unfavorable interaction, which may decrease binding stability [26]. Liquiritin engages in hydrophobic (Pi-Alkyl) and electrostatic interactions, though unfavorable acceptor-acceptor interactions at certain sites reduce binding efficiency [24]. Glabridin\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003ebinds through hydrophobic interactions (Pi-Alkyl) and electrostatic Pi-Anion bonds with Glutamic acid, contributing to stability [26].\u003c/p\u003e\n\u003cp\u003eThe interactions between licorice compounds with ZYMV-NIb involve a mix of hydrophobic and electrostatic forces that stabilize the protein-ligand complexes and influence binding specificity. Glycyrrhetic acid forms strong hydrophobic interactions (alkyl, Pi-Alkyl) with residues like Leucine, Valine, and Methionine, alongside electrostatic stabilization via hydrogen bonds with Serine and Lysine. However, an unfavorable donor-donor interaction with Arginine may weaken binding at this site [28]. Isoliquiritin shows hydrophobic (Pi-Sigma, Pi-Alkyl) and electrostatic (hydrogen) interactions. However, the donor-donor interaction with Serine at A:254 reduces stability at this site [26], although other interactions stabilize the complex, such as Pi-Alkyl with Lysine and Arginine [24].\u003c/p\u003e\n\u003cp\u003eLiquiritin forms hydrophobic (Pi-Alkyl, Pi-Sigma) and electrostatic interactions with residues like Leucine, Tyrosine, and Aspartic acid. However, weak interactions at some sites, like Glutamic acid, may limit binding efficiency [28]. Glabridin primarily forms hydrophobic alkyl interactions with Arginine and Lysine, alongside hydrogen bonds, to stabilize the complex [24].\u003c/p\u003e\n\u003cp\u003eThe interactions between these compounds with ZYMV-CP involve a combination of hydrophobic and electrostatic forces that contribute to the stability and specificity of the protein-ligand complexes. Glycyrrhetic acid primarily forms hydrophobic interactions (alkyl, Pi-Alkyl) with residues like Alanine, Phenylalanine, and Lysine, anchoring it within the protein\u0026apos;s hydrophobic pocket. Additionally, Lysine forms hydrogen bonds, contributing to electrostatic stabilization [28]. Isoliquiritin interacts via Pi-Alkyl bonds with Lysine, while hydrogen bonds with Proline and favorable interactions with Lysine and Aspartic acid further stabilize the complex. However, an unfavorable donor-donor interaction with Arginine weakens binding at this site [24, 26].\u003c/p\u003e\n\u003cp\u003eLiquiritin forms a combination of hydrophobic and electrostatic interactions, such as Pi-Alkyl bonds with Alanine and hydrogen bonds with Asparagine and Phenylalanine. The presence of unfavorable donor-donor interactions with Arginine suggests certain regions may be suboptimal for binding [28]. Glabridin binds through hydrophobic interactions (Pi-Sigma, alkyl) with Alanine, along with hydrogen and Pi-Cation bonds from Aspartic acid, and Pi-Anion interactions with Arginine. These forces stabilize the ligand primarily through non-polar interactions [24]. In a conclusion, hydrophobic interactions, particularly alkyl, Pi-Alkyl, and Pi-Sigma bonds, dominate the binding of these compounds to ZYMV-CP. Electrostatic hydrogen bonds also contribute to stability, though unfavorable donor-donor interactions in some regions may weaken the binding.\u0026nbsp;\u003c/p\u003e"},{"header":"Conclusion","content":"\u003cp\u003eLicorice-derived bioactive compounds demonstrate strong potential as antiviral agents due to their ability to form stable protein-ligand complexes with ZYMV proteins. Hydrophobic interactions, such as alkyl and Pi-based bonds, play a central role in stabilizing these complexes, while electrostatic hydrogen bonds further enhance binding affinity and specificity. Though some unfavorable interactions suggest opportunities for optimization, modifying these compounds can improve their antiviral potential. Overall, these natural compounds offer a promising alternative to synthetic drugs and could serve as the basis for more targeted, effective therapies against ZYMV and related viruses.\u003c/p\u003e"},{"header":"Abbreviations","content":"\u003cp\u003eZYMV; Zucchini yellow mosaic virus, PDB; Protein Data Bank, 2D; Two D structure, 3D; Three D structures, GLY; Glycine, THR; Threonine, VAL; Valine, LYS; Lysine, GLU; Glutamic acid, ARG; Arginine, TYR; Tyrosine, GLN; Glutamine, PHE; Phenylalanine, SER; Serine, HIS; Histidine, LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e;\u003c/span\u003e\u003c/strong\u003e Leucine, ASP; Aspartic acid, ASN; Asparagine, CYS; Cysteine, ILE; IsoLeucine, ALA; Alanine, PRO; Proline, TRP; Tryptophan, and MET; Methionine.\u003c/p\u003e"},{"header":"Declarations","content":"\u003cp\u003e\u003cstrong\u003eEthics approval and consent to participate\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThis study involved only plant and microbial samples, which do not require ethical approval under current research guidelines for human or animal subjects.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eConsent for Publication\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eNot applicable. This study does not involve any personal data or information requiring consent for publication.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eAvailability of data and material\u003c/strong\u003e\u003cstrong\u003es\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eNo new datasets were generated or analyzed during the course of this study.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eCompeting Interests\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe authors declare no competing interests. There are no financial, personal, or professional relationships that could have influenced the outcomes of this study.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eFunding\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe authors declare that no funding, grants, or other financial support was received for the preparation of this manuscript.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eAuthors\u0026rsquo; contributions\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eShrouk E.E. Farag conceptualized the study, gathered molecular nucleotide data, performed genetic variability analysis of ZYMV, and drafted the initial manuscript. Shafik D. Ibrahim carried out the protein-level analyses, evaluated genetic diversity using protein sequences, interpreted findings, and participated in manuscript revision. Atef S. Sadik oversaw the research process, ensured methodological rigor, contributed to the study design, and was actively involved in reviewing and approving the final manuscript. Mamdouh H. Abdel-Gaffar provided expertise in bioinformatics and phylogenetic analysis, supported the comparative genomics component, and contributed to the study design and manuscript development.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eAcknowledgments\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe authors extend their sincere gratitude to Miss El-Shymaa Tarek for her valuable assistance with the molecular docking analysis. Her guidance and support throughout the research process were greatly appreciated.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eClinical Trial Number\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eNot applicable\u003c/p\u003e"},{"header":"References","content":"\u003col\u003e\n\u003cli\u003eAhsan M, Ashfaq M, Amer MA, Shakeel MT, Mehmood MA, Umar M, et al. \u003cem\u003eZucchini yellow mosaic virus\u003c/em\u003e (ZYMV) as a serious biotic stress to cucurbits: prevalence, diversity, and its implications for crop sustainability. Plants, 2023;12(19):3503.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003ehttps://doi.org/10.3390/plants12193503\u003c/li\u003e\n\u003cli\u003eAl-Tamimi N, Kawas H, Mansour A, Salem N. Biological and molecular characterization of some \u003cem\u003eZucchini yellow mosaic virus\u003c/em\u003e isolates from Southern Syria and Jordan valley. Jordan Journal of Agricultural Sciences, 2010;6(3):1-15.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eKamal R, Gusain YS, Kumar V, Sharma AK. Disease management through biological control agents: An eco-friendly and cost effective approach for sustainable agriculture-A Review. Agricultural Reviews, 2015;\u003cem\u003e36\u003c/em\u003e(1):37-45.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eVelasco L, Ruiz L, Galipienso L, Rubio L, Janssen D. A historical account of viruses in intensive horticultural crops in the Spanish Mediterranean Arc: New challenges for a sustainable agriculture. Agronomy, 2020;10(6):1-26. \u003c/li\u003e\n\u003cli\u003eSrivastava RM, Joshih S. Integrated pest management for cucurbits in cucumber (\u003cem\u003eCucumis sativus\u003c/em\u003e L.). Cucumber Economic Values and Its Cultivation and Breeding, 2021;1(5):1-10.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eBaldodiya GM, Saikia R, Paswan RR, Borah BK. Sustainable agriculture and viral diseases of plants: An overview. New and Future Developments in Microbial Biotechnology and Bioengineering, 2022;419-434.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eJoseph J, N., Shrivastava, A., Benny, B., Baig, M. Y., Georgine S, A., \u0026amp; Saral A, M. (2023). Antiviral properties of various bioactive components present in the root of Glycyrrhiza glabra. \u003cem\u003eCurrent Nutrition \u0026amp; Food Science\u003c/em\u003e, 19(2), 166-175.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eParizipour MG, Shahriari AG. Investigation of antiviral potential of licorice (\u003cem\u003eGlycyrrhiza glabra\u003c/em\u003e L.) crude extract against \u003cem\u003eTobacco mosaic virus\u003c/em\u003e. J. Anim. Plant Sci, 2020;30(1):107-114.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eGomaa AA, Abdel-Wadood YA. The potential of glycyrrhizin and licorice extract in combating COVID-19 and associated conditions. Phytomedicine plus, 2021;1(3):1-12.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eElshaer NA, El-Masry SS, Rabiee MS, Sadik AS, Megahed AA. In Silico prediction of the potential of some bioactive compounds from Licorice to target \u003cem\u003eBanana bunchy top virus\u003c/em\u003e. Egyptian Journal of Phytopathology, 2025;53(1):194-224.\u003c/li\u003e\n\u003cli\u003eJakhar R, Dangi M, Khichi A, Chhillar AK. Relevance of molecular docking studies in drug designing. Current Bioinformatics, 2020;\u003cem\u003e15\u003c/em\u003e(4):270-278.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eMahmud S, Uddin MAR, Paul GK, Shimu MSS, Islam S, Rahman E, et al. Virtual screening and molecular dynamics simulation study of plant-derived compounds to identify potential inhibitors of main protease from SARS-CoV-2. Briefings in bioinformatics, 2021;22(2):1402-1414.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eJamal QMS. Antiviral potential of plants against COVID-19 during outbreaks-An update. International Journal of Molecular Sciences, 2022;23(21):1-25.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eH\u0026yacute;skov\u0026aacute; V, Bělonožn\u0026iacute;kov\u0026aacute; K, Chmel\u0026iacute;k J, Hoffmeisterov\u0026aacute; H, Čeřovsk\u0026aacute; N, Moravec T, et al. Potyviral helper-component protease: Multifaced functions and interactions with host proteins. Plants, 2024;13(9):1236.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e https://doi.org/10.3390/plants13091236\u003c/li\u003e\n\u003cli\u003eGohlke H, Klebe G. Approaches to the description and prediction of the binding affinity of small‐molecule ligands to macromolecular receptors. Angewandte Chemie International Edition, 2002;41(15):2644-2676.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eAseel DG, Rabie M, El-Far A, Abdelkhalek A. Antiviral properties and molecular docking studies of eco-friendly biosynthesized copper oxide nanoparticles against alfalfa mosaic virus. BMC Plant Biology, 2024;24(1):1-16.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003ehttps://link.springer.com/article/10.1186/s12870-024-05802-1\u003c/li\u003e\n\u003cli\u003eKitchen DB, Decornez H, Furr JR, Bajorath J. Docking and scoring in virtual screening for drug discovery: Methods and applications. Nature reviews Drug discovery, 2004;3(11):935-949.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eKhan T, Raza S. Exploration of computational aids for effective drug designing and management of viral diseases: A comprehensive review. Current Topics in Medicinal Chemistry, 2023;23(17):1640-1663.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eKirchmair J, Distinto S, Roman Liedl K, Markt P, Maria Rollinger J, Schuster D, et al. Development of anti-viral agents using molecular modeling and virtual screening techniques. Infectious Disorders-Drug Targets (Formerly Current Drug Targets-Infectious Disorders), 2011;11(1):64-93.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eAzeem M, Mustafa G, Ahmed S, Mushtaq A, Arshad M, Usama M, et al. Structure based screening and molecular docking with dynamic simulation of natural secondary metabolites to target RNA-dependent RNA polymerase of five different retroviruses. Plos one, 2024;19(8):e0307615.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003ehttps://doi.org/10.1371/journal.pone.0307615\u003c/li\u003e\n\u003cli\u003eBai Q, Jiang J, Luo D, Huang Y, Huang M, Zhao G, et al. Cysteine protease domain of Potato Virus Y: The potential target for urea derivatives. pestic. biochem. Physiol., 189, 2023;105309. https://doi.org/10.1016/j.pestbp.2022.10530\u003c/li\u003e\n\u003cli\u003eBallester PJ, Mitchell JB. A machine learning approach to predicting protein\u0026ndash;ligand binding affinity with applications to molecular docking. Bioinformatics, 2010;26(9):1169-1175.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003ehttps://doi.org/10.1093/bioinformatics/btq112\u003c/li\u003e\n\u003cli\u003eChoudhury C, Narahari Sastry G. Pharmacophore modelling and screening: Concepts, recent developments and applications in rational drug design. Structural bioinformatics: applications in preclinical drug discovery process, 2019;25-53.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eBrylinski M. Aromatic interactions at the ligand\u0026ndash;protein interface: Implications for the development of docking scoring functions. Chemical biology \u0026amp; drug design, 2018;91(2):380-390.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003ehttps://doi.org/10.1111/cbdd.13084\u003c/li\u003e\n\u003cli\u003eWang X, Song K, Li L, Chen L. Structure-based drug design strategies and challenges. Current Topics in Medicinal Chemistry, 2018;18(12):998-1006.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003ede Sousa Luis JA, Barros RP, de Sousa NF, Muratov E, Scotti L, Scotti MT. Virtual screening of natural products database. Mini Reviews in Medicinal Chemistry, 2021;21(18):2657-2730.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003cli\u003eGhildiyal R, Prakash V, Chaudhary VK, Gupta V, Gabrani R. Phytochemicals as antiviral agents: Recent updates. Plant-Derived Bioactives: Production, Properties and Therapeutic Applications, 2020;279-295.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e \u003c/li\u003e\n\u003cli\u003eLiu L, Bagal D, Kitova EN, Schnier PD, Klassen JS. Hydrophobic protein\u0026minus;ligand interactions preserved in the gas phase. Journal of the American Chemical Society, 2009;131(44):15980-15981.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e \u003c/li\u003e\n\u003cli\u003eLi T, Ayers PW, Liu S, Swadley MJ, Aubrey‐Medendorp C. Crystallization force\u0026mdash;a density functional theory concept for revealing intermolecular interactions and molecular packing in organic crystals. Chemistry\u0026ndash;A European Journal, 2009;15(2):361-371.\u003cspan dir=\"RTL\"\u003e\u0026rlm;\u003c/span\u003e\u003c/li\u003e\n\u003c/ol\u003e"},{"header":"Tables","content":"\u003cp\u003e\u003cstrong\u003eTable 1\u0026nbsp;\u003c/strong\u003eMolecular docking and binding affinities of four licorice compounds against ZYMV protein.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd rowspan=\"2\" valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003e\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e\u003c/p\u003e\n \u003cp\u003e\u003cstrong\u003eLigands\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"10\" valign=\"top\" style=\"width: 511px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eZYMV-protein\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eP1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eHC-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eP3\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e\u003cstrong\u003e6K1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eCI\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e\u003cstrong\u003e6K2\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eNIa-VPg\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eNIa-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eNIb\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eCP\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"11\" valign=\"top\" style=\"width: 624px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eMolecular docking\u0026nbsp;\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eGlycyrrhetic acid\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-9.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-7.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-7.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-6.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-7.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-8.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-8.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.4\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eIsoliquiritin\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-8.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-7.0\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-5.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-8.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-7.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-7.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eLiquiritin\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-9.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-7.0\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-6.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-9.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-6.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-7.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-8.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-8.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.5\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eGlabridin\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-8.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-6.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-6.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-6.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-8.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-8.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-8.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"11\" valign=\"top\" style=\"width: 624px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eControl\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eAcyclovir\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-6.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-5.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-5.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-4.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-5.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-3.9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-5.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-5.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-5.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-4.6\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"11\" valign=\"top\" style=\"width: 624px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eBinding affinities\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eGlycyrrhetic acid\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-9.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-7.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.0\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-7.0\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-6.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-7.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-8.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-9.0\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.9\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eIsoliquiritin\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-8.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-7.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-5.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-8.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-7.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-7.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.2\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eLiquiritin\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-9.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-7.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-6.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-7.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-8.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-8.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.4\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eGlabridin\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-9.0\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-6.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-6.2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-6.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-8.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-6.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-8.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-8.1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-8.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"11\" valign=\"top\" style=\"width: 624px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eControl\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 113px;\"\u003e\n \u003cp\u003eAcyclovir\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 37px;\"\u003e\n \u003cp\u003e-6.3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 54px;\"\u003e\n \u003cp\u003e-5.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 43px;\"\u003e\n \u003cp\u003e-5.7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 41px;\"\u003e\n \u003cp\u003e-4.6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-5.9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 48px;\"\u003e\n \u003cp\u003e-3.8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 72px;\"\u003e\n \u003cp\u003e-4.4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 66px;\"\u003e\n \u003cp\u003e-5.9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-5.5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 51px;\"\u003e\n \u003cp\u003e-4.4\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u003cstrong\u003eTable 2\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-P1 Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-P1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLY\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1447\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1472\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1278\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1345\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1492\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1493\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-P1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1805\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1505\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1806\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1754\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1803\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Acceptor-Acceptor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1801\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-P1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1633\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1807\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon- H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1631\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1786\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1635\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1429\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1433\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Unfavorable Acceptor-Acceptor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-P1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1426\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1631\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Pi Stacked, Pi-Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1786\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1660\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:1633\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon- H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-P1: Zucchini yellow mosaic virus-P1; GLY: Glycine; THR: Threonine; VAL: Valine; LYS: Lysine; GLU: Glutamic acid; ARG: Arginine; TYR: Tyrosine; GLN: Glutamine; PHE: Phenylalanine; SER: Serine; HIS: Histidine; LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine; ASP: Aspartic acid; and ASN: Asparagine.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 3\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-HC-Pro Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"4\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-HC-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eCYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:342\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:417\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl, Carbon- H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:335\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:337\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"4\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-HC-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:352\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:335\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:432\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:430\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:349\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:401\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Pi-Anion, PI Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"4\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-HC-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:335\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:415\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLY\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:456\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:416\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eCYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:342\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sulfur\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:417\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"4\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-HC-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:419\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:401\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Anion\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:418\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Anion\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:349\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:352\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:403\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"2\" valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:404\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd style=\"width: 90px;\"\u003e\u003cbr\u003e\u003c/td\u003e\n \u003ctd style=\"width: 5px;\"\u003e\u003cbr\u003e\u003c/td\u003e\n \u003ctd style=\"width: 97px;\"\u003e\u003cbr\u003e\u003c/td\u003e\n \u003ctd style=\"width: 432px;\"\u003e\u003cbr\u003e\u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-HC-Pro: Zucchini yellow mosaic virus-HC-Pro; CYS: Cysteine; ILE: Isoleucine; TYR: Tyrosine; ALA: Alanine; VAL: Valine; LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine; GLU: Glutamate; HIS: Histidine; GLY: Glycine; SER: Serine; ASP: Aspartic acid ; PRO: Proline; \u0026nbsp;and ARG: Arginine.\u0026nbsp;\u003cbr\u003e\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 4\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-P3 Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-P3\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:304\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:305\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:307\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:322\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Sigma, Carbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:327\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-P3\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:329\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:327\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:305\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:322\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:325\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-P3\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:307\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:322\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen, Pi-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:327\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:305\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-P3\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:327\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:329\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Anion\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:305\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Alkyl, Carbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:322\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Pi-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 94px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 97px;\"\u003e\n \u003cp\u003eA:325\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Unfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-P3: Zucchini yellow mosaic virus-P3; HIS: Histidine; ILE: Isoleucine; SER: Serine; ARG: Arginine; ASP: Aspartic acid; and ASN: Asparagine.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 5\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-6K1 Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-6K1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:23\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:34\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Alkyl, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:32\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-6K1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:24\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:27\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:23\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Pi T-Shaped\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:34\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-6K1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:37\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:27\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:23\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Pi T-Shaped\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:34\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-6K1\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:34\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:41\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:38\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:15\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:37\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl, Pi-Alkyl, Pi-Alkyl, Pi-Cation\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:16\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:35\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-6K1: Zucchini yellow mosaic virus-6K1; PHE: Phenylalanine; ILE: Isoleucine; ASP: Aspartic acid; ARG: Arginine; LYS: Lysine; VAL; Valine; and LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine. \u0026nbsp;\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 6\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-CI Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-CI\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:207\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:179\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:376\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:378\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:177\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:205\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Donor-H, Carbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-CI\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:205\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Donor-H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:207\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:376\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:209\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:187\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Unfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-CI\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLY\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:208\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Pi-Donor-H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:207\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:205\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Donor-H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:310\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:187\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-CI\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:207\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:179\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Donor-H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:376\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Donor-H\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:378\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl, Pi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eHIS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:177\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:205\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Donor-H, Carbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-CI: Zucchini yellow mosaic virus-CI; PRO: Proline; THR: Threonine; SER: Serine; HIS: Histidine; ARG: Arginine; ASN: Asparagine; and GLY; Glycine\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 7\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-6K2 Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-6K2\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTRP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:36\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-6K2\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:22\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Unfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTRP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:15\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:19\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:23\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Anion, Conventional Hydrogen, Unfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-6K2\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLY\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:33\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003evan der Waals\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eMET\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD: 29\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:32\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAmide-Pi Stacked, Amide-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-6K2\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:19\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTRP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eD:15\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Alkyl, Alkyl, Pi-Pi Stacked\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-6K2: Zucchini yellow mosaic virus-6K2; TRP: Tryptophan; ASN: Asparagine; LYS: Lysine; ASP: Aspartic acid; GLY; Glycine; MET: Methionine; and LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 8\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-NIa-VPg Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-NIa-VPg\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:143\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:96\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:93\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:124\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:141\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-NIa-VPg\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:78\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:91\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Acceptor-Acceptor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:89\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:124\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-NIa-VPg\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:121\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:78\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:141\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:124\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL \u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:96\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:93\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-NIa-VPg\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:141\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:124\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Alkyl, Pi-Alkyl, Pi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE \u0026nbsp;\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:93\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Alkyl, Pi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:96\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-NIa-VPg: Zucchini yellow mosaic virus-NIa-VPg; PRO: Proline; VAL; Valine; ILE: Isoleucine; LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine; ASP: Aspartic acid; THR: Threonine; and LYS: Lysine.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 9\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-NIa-Pro Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-NIa-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp dir=\"RTL\"\u003e\u003cspan dir=\"LTR\"\u003eLYS\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp dir=\"RTL\"\u003e\u003cspan dir=\"LTR\"\u003eA:6\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp dir=\"RTL\"\u003e\u003cspan dir=\"LTR\"\u003eConventional Hydrogen\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:11\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:125\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-NIa-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u0026nbsp;ALA\u0026nbsp;\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:170\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLY\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:168\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:29\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Acceptor-Acceptor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:146\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-NIa-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:220\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Acceptor-Acceptor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:30\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:170\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eCYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:151\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:147\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:146\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:221\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:29\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-NIa-Pro\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:148\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Anion\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:170\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-NIa-Pro: Zucchini yellow mosaic virus-Nia-Pro; LYS: Lysine; TYR: Tyrosine; VAL; Valine; ALA: Alanine; GLY; Glycine; THR: Threonine; GLU: Glutamic acid; CYS: Cysteine; ASN: Asparagine; and GLN: Glutamine\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 10\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-NIb Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-NIb\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:122\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:152\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:121\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:202\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eCYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:203\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eMET\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:281\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:119\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:140\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:148\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:135\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:198\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-NIb\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTHR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:81\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:184\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:254\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:253\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:352\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:187\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:185\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-NIb\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:116\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eILE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:118\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:121\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:198\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eTYR\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:119\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Pi T-Shaped\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:202\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eVAL\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:204\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:205\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:206\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:207\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eCarbon Hydrogen, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-NIb\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eSER\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:310\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:187\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:185\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:304\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-NIb: Zucchini yellow mosaic virus-NIb; LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine; SER: Serine; VAL; Valine; CYS: Cysteine; MET: Methionine; TYR: Tyrosine; PHE: Phenylalanine; ARG: Arginine; LYS: Lysine; GLU: Glutamic acid; THR: Threonine; ASN: Asparagine; ASP: Aspartic acid; ARG: Arginine; and PHE: Phenylalanine.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 11\u0026nbsp;\u003c/strong\u003eBonding Interactions of Amino Acid Residues in ZYMV-CP Protein with Four Licorice-Derived Bioactive Compounds.\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"0\" cellpadding=\"0\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eAmino acids\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eSites\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eTypes of bonds\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlycyrrhetic acid-ZYMV-CP\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eB:39\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl, Pi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:44\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:36\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:34\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eAlkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eIsoliquiritin-ZYMV-CP\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:41\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:38\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:42\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLYS\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:44\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl, Conventional Hydrogen, Pi-Anion\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:30\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Cation\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eLEU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:29\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eLiquiritin-ZYMV-CP\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:23\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eUnfavorable Donor-Donor, Conventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASN\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eB:37\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePHE\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:31\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eB:39\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eB:42\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eGLU\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eC:26\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Conventional Hydrogen, Carbon Hydrogen\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd colspan=\"3\" valign=\"top\" style=\"width: 623px;\"\u003e\n \u003cp\u003e\u003cstrong\u003eGlabridin-ZYMV-CP\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:39\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Sigma, Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eASP\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eB:30\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003eConventional Hydrogen, Pi-Cation\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eARG\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:42\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Anion\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003eALA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eB:27\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd valign=\"top\" style=\"width: 90px;\"\u003e\n \u003cp\u003ePRO\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 102px;\"\u003e\n \u003cp\u003eA:38\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd valign=\"top\" style=\"width: 432px;\"\u003e\n \u003cp\u003ePi-Alkyl\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eNotes: ZYMV-CP: Zucchini yellow mosaic virus-CP; ALA, Alanine; LYS, Lysine; PHE, Phenylalanine; PRO: Proline; ARG: Arginine; ASP: Aspartic acid; LEU\u003cstrong\u003e\u003cspan dir=\"RTL\"\u003e:\u003c/span\u003e\u003c/strong\u003e Leucine; ARG: Arginine; ASN: Asparagine; PHE: Phenylalanine); and GLU: Glutamic Acid (Glutamate)\u003c/p\u003e"},{"header":"Figures","content":"\u003cp\u003eThe cited figures are not available with this version.\u003c/p\u003e"}],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":true,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":false,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":false,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"Antiviral drug development, Binding affinity, Licorice, Molecular docking, Protein-ligand interactions, ZYMV","lastPublishedDoi":"10.21203/rs.3.rs-7011143/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-7011143/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"This study investigates the molecular docking and binding affinities of four licorice-derived bioactive compounds against 10 proteins of Zucchini yellow mosaic virus (ZYMV), including P1, HC-Pro, P3, 6K1, 6K2, CI, NIa-VPg, NIa-Pro, and NIb. ZYMV is a significant viral pathogen affecting cucurbit crops worldwide, leading to major economic losses. Traditional antiviral strategies have limitations, and bioactive compounds derived from plants have gained attention for their potential to inhibit viral activity. The docking scores reveal that Glycyrrhetic acid and Liquiritin demonstrate the strongest binding, particularly to the P1 target, while Isoliquiritin shows weaker binding. Acyclovir, the control drug, exhibited the least effective binding across all targets. The bonding interactions between the compounds and ZYMV proteins involve a combination of hydrophobic (alkyl, Pi-Alkyl, Pi-Sigma), electrostatic (hydrogen bonds, Pi-Cation, Pi-Anion), and aromatic (Pi-Pi) interactions, each contributing to the stability of the protein-ligand complexes. Glycyrrhetic acid and Liquiritin primarily engage in hydrophobic interactions, enhancing their binding stability, while Isoliquiritin and Glabridin also form electrostatic and aromatic interactions. Some unfavorable interactions, such as donor-donor or acceptor-acceptor bonds, were identified, indicating potential regions for optimization in ligand binding. These findings highlight the promising antiviral potential of licorice-derived compounds, particularly Glycyrrhetic acid and Liquiritin, as inhibitors of ZYMV. The results emphasize the role of non-polar interactions in stabilizing the binding complexes, suggesting these compounds could modulate protein function. The study provides valuable insights for future antiviral drug development, with potential strategies to optimize binding affinity and enhance the efficacy of licorice-derived bioactive compounds in targeting ZYMV.","manuscriptTitle":"Assessment of Antiviral Activities of Four Licorice Compounds against Zucchini Yellow Mosaic Virus through Molecular Docking","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2025-07-14 15:22:17","doi":"10.21203/rs.3.rs-7011143/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"d6a8c570-532d-4bf6-bb7e-2cdca87dbe81","owner":[],"postedDate":"July 14th, 2025","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[],"tags":[],"updatedAt":"2025-07-30T13:39:23+00:00","versionOfRecord":[],"versionCreatedAt":"2025-07-14 15:22:17","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-7011143","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-7011143","identity":"rs-7011143","version":["v1"]},"buildId":"8U1c8b4HqxoKbykW_rLl7","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}