Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry

Immunoglobulin light chains, a component of antibodies, can misfold and aggregate to cause systemic AL amyloidosis. Aggregation, including amyloid fibril formation, requires unfolding of the full-length light chain from its native state, and in most cases aberrant proteolysis. Small molecules that bind to the native state of light chains to stabilize them against conformational excursions and proteolysis are under development as drug candidates for AL amyloidosis. Since each patient has a unique light chain sequence, a challenge for candidate stabilizer drugs is to bind multiple light chains and suppress their dynamics. Here, we used hydrogen-deuterium exchange measured by mass spectrometry to characterize the binding of six small molecule stabilizers to eleven different λ light chain proteins. Despite structural and dynamic differences among the light chains, the binding of the most efficacious stabilizer molecule led to increased protection from hydrogen exchange, consistent with reduced local and global unfolding. Protection upon binding was most prominent in residues within complementarity determining region 3 and framework region 4 of the light chain variable domains, which undergo major conformational changes enabling amyloid formation. Stabilizer binding also reduced the rate at which all light chains were cleaved by protease. These data show that these stabilizers suppress the range of conformational dynamics associated with light chain aggregation, supporting their therapeutic potential.

Immunoglobulin light chain amyloidosis; AL amyloidosis; amyloid fibrils; Light chain kinetic stabilizers; drug design; protein stability and dynamics; HDX-MS; PLIMSTEX analysis. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Highlights • Small-molecule kinetic stabilizers suppress conformational dynamics and aberrant proteolysis of diverse amyloidogenic full-length λ light chains. • HDX-MS indicates conserved protection in regions forming the interface between the two variable domains of the light chain dimer, corresponding to residues that form the core of patient-derived amyloid fibrils. • PLIMSTEX binding titrations show coupled binding, dimerization and stabilization at sub- micromolar kinetic stabilizer concentrations. • Small molecule kinetic stabilization across different λ sequences supports kinetic stabilizers as a promising therapeutic strategy for AL amyloidosis. Declaration of interests: NLY, JWK and GJM are authors on a patent that describes the use of kinetic stabilizers as a potential therapy for AL amyloidosis. JWK is a founder and board member of Protego Biopharma. Abbreviations: AL – amyloid light chain; CDR – complementarity determining region; CL – light chain constant domain; FL – full-length; FR – framework region; HDX – hydrogen-deuterium exchange; GL – germline; LC – immunoglobulin light chain; MM – multiple myeloma; MS – mass spectrometry; SDS PAGE – sodium dodecyl sulfate polyacrylamide gel electrophoresis; ThT - thioflavin T; VL – light chain variable domain. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint

Unfolding and subsequent aberrant proteolysis of full-length (FL) immunoglobulin light chain (LC) proteins are generally required for the formation of amyloid light chain (AL) deposits in the disease AL amyloidosis (Figure 1A), one of a spectrum of systemic amyloidoses (Buxbaum et al. 2024). Accumulation of amyloid fibrils derived from normally soluble LCs in multiple tissues leads to progressive and eventually fatal organ dysfunction (Sanchorawala 2024; Merlini et al. 2018). Soluble, misfolded LCs can also contribute to cardiotoxicity that is the major cause of mortality (Merlini et al. 2018). FL LCs are subunits of antibodies that normally function in the immune system to recognize antigens (Del Pozo-Yauner et al. 2023). Antibodies are covalent heterotetramers of two FL LCs and two heavy chains, which circulate in blood alongside “free” LC monomers and homodimers— FL LCs are produced in excess to enable efficient antibody secretion (Feige, Hendershot, and Buchner 2010). Overproduction of a single monoclonal free LC by an aberrant clonal cell population can cause LC fragment accumulation as amyloid fibrils within tissues. Each AL patient has an essentially unique LC sequence that forms amyloid (Morgan et al. 2025). The amino acid sequence of each LC appears to define its propensity to aggregate (Del Pozo-Yauner et al. 2023; Absmeier et al. 2023). Amyloid formation is also driven, in part, by increased concentration of the monoclonal free FL LC or fragments thereof, so existing therapies kill the clonal cells to reduce the total amyloidogenic LC concentration (Sanchorawala 2024; Merlini et al. 2018). Protein conformational control by small molecules that modulate protein assembly, folding and stability have become an important class of drugs, targeting proteins associated with multiple disease categories (Chiti and Kelly 2022). Kinetic stabilizers are a subset of these molecules, which selectively bind to the native state and slow the rate of protein unfolding. Kinetic stabilization of circulating LCs should protect residual free LCs from misfolding, aberrant proteolysis and aggregation, thus complementing cytotoxic chemotherapies (Morgan, Buxbaum, and Kelly 2021), and this concept is currently being tested in clinical trials. There are two types of LC, κ and λ, of which λ LCs are more frequently involved in AL amyloidosis (Kourelis et al. 2017; Merlini et al. 2018; Morgan et al. 2025). FL LCs are secreted as 210–220-residue proteins that fold into two independent structural domains (Figure 1A), a variable (V L) domain and a constant (CL) domain (Del Pozo-Yauner et al. 2023; Feige, Hendershot, and Buchner 2010). Both domains have a ß-sandwich structure, termed an immunoglobulin (Ig) fold, stabilized by an intramolecular disulfide bond. The N-terminal variable domain (residues 1–113 in the alignment shown in Figures 1B and 1C) is involved in antigen binding when incorporated into antibodies via three highly polymorphic .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint loops known as complementarity determining regions (CDR, Figure 1C). Other residue segments, defined as framework regions (FR), are more conserved. The C-terminal constant LC domain (residues 114-219) has a structural role within antibodies, and its sequence is highly conserved between LCs. Free FL LCs can form homodimers in circulation. Such free LC dimers have a parallel orientation where the VL and CL domains from one protomer interact with their counterpart in the other protomer (Figure 1A). Residues from ß-strands CV, C’V, FV and GV form a VL-VL interface, while residues from ß-strands AC, BC, DC and EC form the CL-CL interface. A cysteine residue near the C-terminus of CL (referred to here as C218, relative to the alignment) can make an intermolecular disulfide bond within the homodimer. In patients, amyloidogenic FL LCs can form both monomers and homodimers (Connors et al. 2007; Andrich et al. 2017; Sternke-Hoffmann et al. 2020). The structured cores of patient-derived amyloid fibrils primarily comprise residues from the VL domain in non-native, cross-ß-sheet conformations (Radamaker et al. 2019). Isolated VL domains can aggregate under mild conditions in vitro, whereas FL LCs remain soluble for extended periods under the same conditions and are much more resistant to aggregation (Morgan and Kelly 2016; Blancas-Mejía et al. 2015; Blancas-Mejía and Ramirez-Alvarado 2016). Amyloid-associated VL domains tend to unfold and aggregate more readily than non-AL VL domains (Wall et al. 1999; Hurle et al. 1994; Baden, Randles, et al. 2008; Kazman et al. 2020; Absmeier et al. 2023). Furthermore, amyloid-associated FL LCs are generally less conformationally stable than their non-AL counterparts and are more prone to local or global unfolding that enables aberrant endoproteolysis, releasing aggregation-prone fragments, including the VL domain (Klimtchuk et al. 2010; Morgan and Kelly 2016; Oberti et al. 2017; Blancas-Mejía et al. 2017; Lavatelli et al. 2024). In some cases, proteolysis can occur after aggregation (Lavatelli et al. 2020). Amyloid fibrils formed by VL domains can accelerate, or seed, the aggregation of full-length LCs (Blancas-Mejía and Ramirez-Alvarado 2016). Collectively, these data suggest a role for the local conformational dynamics in sensitive protein regions. These regions have been proposed to involve: i) domain-domain interfaces in free LCs, such as the VL-VL and VL-CL interfaces (Rennella et al. 2019; Brumshtein et al. 2014; Baden, Owen, et al. 2008); ii) regions involving the internal disulfide bond in VL, a region that unfolds during amyloid formation (Radamaker et al. 2019; Klimtchuk et al. 2023); iii) amyloid-promoting regions (APRs), which are sequence regions with high intrinsic aggregation propensity that are proposed to initiate protein misfolding (Klimtchuk et al. 2023; Peterle et al. 2021; Goldschmidt et al. 2010); iv) mutation, misfolding or proteolysis of the C L domains (Klimtchuk et al. 2010; Benson, Liepnieks, and Kluve-Beckerman 2015; Morgan, Usher, and .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Kelly 2017; Rottenaicher et al. 2023; Lavatelli et al. 2024). The roles of these sensitive regions in amyloid formation may differ for different LC sequences, complicating their therapeutic targeting. Because LCs have diverse sequences and no natural small-molecule ligands, historically they epitomized a challenging drug target (Yan et al. 2023). Nontheless, we carried out a high-throughput screen that identified small molecules that protect folded FL LCs from undergoing conformational excursions enabling proteolysis, compounds that we call LC kinetic stabilizers; these molecules bind highly conserved residues at the VL-VL interface of the LC homodimer (Morgan et al. 2019) (Figure 1B, colored residues). Subsequent structure-based medicinal chemistry efforts led to more potent kinetic stabilizers (Figure 1D) (Yan et al. 2020, 2021, 2022; Yan, Wilson, and Kelly 2023; Lederberg et al. 2024). Screening and optimization of hit molecules was mainly carried out using a single full-length LC protein, termed WIL-FL. A key challenge for ongoing drug development is to identify kinetic stabilizers that bind tightly and specifically to multiple LCs with diverse sequences. These kinetic stabilizers slow LC unfolding by strengthening the VL-VL domain interface within the LC homodimer, which is expected to decelerate proteolysis and aggregation. However, the effects of small-molecule kinetic stabilizers on localized unfolding and proteolysis of a broader collection of FL LCs associated with amyloidosis have not been scrutinized experimentally. To explore the conformational dynamics of multiple FL LCs we used hydrogen-deuterium exchange (HDX) mass spectrometry (MS). Previously, we used HDX-MS to investigate the native structure and dynamics of isolated VL domains, FL LCs, and IgG proteins to identify specific regions that potentially contribute to protein misfolding enabling aberrant proteolysis (Peterle et al. 2021; Klimtchuk et al. 2023, 2024). In the current study we investigated localized unfolding in nine different FL LCs and the influence that the binding of small-molecule kinetic stabilizers have on these dynamics. The stabilizers explored were either screening hits (e.g. P1 and P5, Figure 1D) or structure-based designed stabilizers (e.g. B20, M63, M53 and M83. We provide molecular details about stabilizers’ mechanism of action and gain insights to guide the development of novel therapies for the treatment of AL amyloidosis.

Protein selection, expression and purification Nine LC proteins selected for analysis are listed in Table 1. Amino acid sequences of these LCs are listed in the Supplementary Information. All residues are numbered according to the sequence alignment shown in Figure 1C. Domain boundaries and CDR residues are defined according to the IMunoGeneTics .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint (IMGT) system (Lefranc et al. 2003). Cysteine 218 in the alignment, which forms an intermolecular disulphide bond, corresponds to residue 214 in the Kabat numbering system (Kabat et al. 1987) and residue 127 of the C-region in the IMGT numbering system. Variable and constant germline genes were assigned using IMGT’s tools for peptide and nucleotide analysis (Lefranc et al. 2018), as appropriate. Each LC listed in Table 1 was expressed as a full-length protein containing Cys218, which predominantly forms disulfide-linked dimers when expressed in E. coli (Peterle et al. 2021). We refer to these tabulated LCs as “AL LC”, “MCG LC”, etc. We also explored two additional proteins: the stand-alone VL domain of the AL sequence (AL VL) and the AL C218S variant (Kabat: C214), where replacement of the cysteine prevents formation of the intermolecular disulfide bond. In total, 11 proteins were studied. Unless otherwise specified, experiments were carried out in phosphate buffered saline (PBS), defined here as 20 mM sodium phosphate buffer, pH 7.4, containing 150 mM NaCl. For proteins where no crystal structure was available, a model was generated using the AlphaFold 3 algorithm, implemented via www.alphafoldserver.com (Abramson et al. 2024). The relative orientations of the V L domains within each model were similar but the “elbow” angle between the VL and CL domains varied; for clarity, only the VL domains are shown when multiple structures are compared. Variants of AL, MM and JTO LCs were expressed in E. coli with N-terminal polyhistidine tags and purified by affinity chromatography as previously described (Peterle et al. 2021). Untagged MCG, H3, H6, H7, H9 and H16 were expressed as inclusion bodies and purified by ion exchange and size exclusion chromatography, as previously described (Oberti et al. 2017; Yan, Wilson, and Kelly 2023). Protein purity was 95%+ verified by SDS-PAGE (Figure S1). Protein molar concentration is reported as monomer equivalents. For LCs characterized to date, stabilizers bind with a stoichiometry of one small molecule to two LC monomers. Small-molecule stabilizers We tested six small-molecule kinetic stabilizers shown in Figure 1D and described in our previous work (Yan et al. 2023): P1, P5, B20, M53, M63 and M83. Numbering corresponds to that from the original paper (Yan et al. 2021). Letters indicate the origin of the molecules: P1 and P5 were originally identified as hits in a high-throughput screen (Morgan et al. 2019); B20, M53, M63 and M83 were designed and synthesized during medicinal chemistry efforts to improve stabilization efficacy (Yan et al. 2021, 2022). These molecules are elaborations on the coumarin scaffold of P1. B20 and M53 retain the original diethylamino substitution in position 7 of the coumarin heterocycle. M63 and M83 incorporate phenylethoxy modifications that were optimized for binding within the core of the LC dimer. Synthesis .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint and purification of these molecules was carried out as previously described (Yan et al. 2021). Small molecules were solubilized in dimethyl sulfoxide (DMSO) vehicle and diluted to the desired concentration. DMSO concentrations were 1.5% during equilibration and 0.15% during deuterium labeling unless otherwise specified. Sequence analysis All AL-associated λ LCs with complete VL domain sequences were taken from AL-Base, available via https://wwwapp.bumc.bu.edu/BEDAC_ALBase/, and aligned according to the IMGT numbering system. Fully conserved gaps, which are used to facilitate structural comparisons between different types of immunoglobulin domains, were removed from the alignment, leaving 113 occupied positions. This alignment was visualized using the ggseqlogo (Wagih 2017) package in R v 4.2.2 (R Core Team 2022), and the binding site residues were highlighted manually. The sequence-based consensus method AmylPred2 (Tsolis et al. 2013) was used to predict the amyloidogenic sequence propensities of the nine LCs under study. APRs are defined as segments predicted by 6 or more of the 10 algorithms available via the AmlyPred2 website. Hydrogen deuterium exchange mass spectrometry (HDX-MS) At least two independent HDX-MS replicates were measured for each LC in accordance with current recommendations (Masson et al. 2019; Engen and Wales 2015). HDX-MS data have been deposited to the ProteomeXchange Consortium via the PRIDE repository (Perez-Riverol et al. 2019) with the dataset identifier PXD068745. Deuterium labeling LCs were freshly diluted to 30 μM in biological replicates from stock concentrations in PBS, pH 7.4, prepared in H2O. Before labeling, the protein solutions were mixed 1-fold with a 300 μM solution of stabilizer molecule in PBS containing 3% (v/v) DMSO. Deuterium labeling commenced with a 10-fold dilution (18 μL) of the D2O labeling buffer (10 mM sodium phosphate, 150 mM NaCl, pD 7.4, 99.9% D2O) added to 2 μL of each 15 μM protein solution. After each labeling time (10 seconds, 1 minute, 10 minutes, 1 hour, 4 hours, 16 hours) at 20 °C, the labeling reaction was quenched with the addition of 20 μL of ice-cold quenching buffer [200 mM sodium phosphate, 4 M guanidine hydrochloride (GdnHCl), 0.72 M TCEP, pH 2.37, H2O] and analyzed immediately by liquid chromatography coupled mass spectrometry (LC-MS). The maximally deuterated samples of each protein that were used for back- exchange correction were prepared as described (Peterle, Wales, and Engen 2022). Protein solutions (15 .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint μL at 15 μM) were lyophilized, resuspended in 7 M GdnHCl containing 50 mM DTT (15 μL), and heated at 90 °C for 5 min. After cooling to 20 °C, 18 μL of labeling buffer (as above) was added to 2 μL of cooled, denatured protein solution, and the exchange reaction was allowed to proceed at 50 °C for 10 min. These maximally deuterated protein samples were then cooled to 0 °C, exchange quenched with the addition of 20 μL of ice-cold quenching buffer (as above) and analyzed immediately by LC-MS. Mass spectrometry LC-MS was performed with a Waters HDX system containing an HDX unit and two Acquity I-class UPLC pumps (Wales et al. 2008). Deuterated and control samples were digested online in the HDX cooling unit, where the digestion chamber was held at 15 °C, using an AffiPro Pepsin column (AffiPro, AP-PC- 001, 2.1 mm × 20 mm). Peptides were trapped and desalted on a VanGuard PreColumn trap [2.1 mm × 5 mm, ACQUITY UPLC BEH C18, 1.7 μm, (Waters, 186002346)] for 3 minutes at 100 μL/min. Peptides were then eluted from the trap using a 5%–35% gradient of acetonitrile over 6 minutes at a flow rate of 100 μL/min, and separated using an ACQUITY UPLC HSS T3, 1.8 μm, 1.0 mm × 50 mm column (Waters, 186003535). The main cooling chamber of the Waters HDX unit, which housed all the chromatographic elements, was held at 0.0 ± 0.1 °C for the entire time of the measurements. The back pressure averaged ~9000 psi at 0 °C and 5% acetonitrile 95% water, 0.1% formic acid. To eliminate peptide carryover, a wash solution (1.5 M GdnHCl, 0.8% formic acid and 4% acetonitrile) was injected over the pepsin column during each analytical run. Mass spectra were acquired using a Waters Synapt XS HDMSE mass spectrometer operated in ion mobility mode. The mass spectrometer was calibrated with direct infusion of a solution of Glu-fibrinopeptide (Sigma, F3261) at 200 femtomole/μL at a flow rate of 5 μL/min prior to data collection. A conventional electrospray source was used, and the instrument was scanned over the range 50 to 2000 m/z. The instrument configuration was: capillary voltage 2.5 kV, trap collision energy at 4 V, sampling cone at 35 V, source temperature of 80 °C, and desolvation temperature of 175 °C. All experiments were done under identical experimental conditions. In this experimental setup, the error in determining peptide deuterium levels was ±0.20 Da, as established using deuterated peptide standards. Data processing Peptides were identified using PLGS 3.0.1 software (Waters, 720001408EN) with replicates of undeuterated samples used as controls. Raw MS data were imported into DynamX 3.0 (Waters, 720005145EN) and filtered with minimum consecutive products of 2 and minimum number of products per amino acid of 0.25. The peptides meeting the filtering criteria were further processed automatically .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint by DynamX followed by manual inspection of all spectra and data processing. The amount of deuterium in each peptide was determined by subtracting the centroid mass of the undeuterated form of each peptide from that of the deuterated form, at each time point, for each condition. Correction for back exchange to report percent deuteration (%D) was done as described (Zhang and Smith 1993) according to the equation: %𝐷𝐷 𝑙𝑙𝑙𝑙𝑙𝑙𝑙𝑙𝑙𝑙= (𝑚𝑚𝑡𝑡− 𝑚𝑚0) (𝑚𝑚𝑚𝑚𝑚𝑚𝑚𝑚𝑚𝑚− 𝑚𝑚0) where mt is the observed peptide centroid mass at a given labeling time-point t, m0 is the undeuterated peptide centroid mass, and mmaxD is the maximally deuterated peptide centroid mass. Peptide-level “chiclet” plot heatmaps were used to visualize the HDX-MS data (Kerres et al. 2017). These visualizations directly show the acquired data, but because the analyzed peptides may not be equivalent between different proteins it can be difficult to make direct comparisons. To more easily visualize differences between LCs, we used the PyHDX web server to reduce the peptide deuteration level information to the single amino acid level (Smit et al. 2021). We assumed that both subunits of the LC dimers were equivalent. All measured and processed values can be found in the Excel supplemental data file. Residue-level percent deuteration values, corrected for back-exchange, were used to generate skyline plots, heat maps, difference heat maps and structural images. Data were plotted onto structural models of the appropriate LC using PyMOL (Schrödinger LLC). For a simple comparison between LCs, we calculated the area under the exchange curve (AUC) over the residues with measurable HDX data in all experiments, using a trapezoidal method. PLIMSTEX analysis of binding affinity Binding affinity between small-molecule stabilizers and proteins was measured by HDX-MS using the PLIMSTEX approach (Zhu et al. 2003). Binding isotherms were generated by incubating 5 μM of protein (AL LC, C218S, or VL) with 2-fold serial dilutions of stabilizer molecules (500 to 1.9 μM) at 20°C in 10 mM sodium phosphate buffer, pH 7.4, containing 150 mM NaCl and 5% DMSO (v/v). After 30 minutes of equilibration at room temperature, 3 μL of the protein-ligand mixture was diluted with 57 μL of deuterium labeling buffer (10 mM sodium phosphate, 150 mM NaCl, pD 7.4, 99.9% D 2O, final DMSO 0.25% v/v) and incubated for 1 hour and 30 minutes at 20°C. After dilution, protein concentration was 0.25 μM and small-molecule stabilizers ranged in concentration from 0.095 to 25 μM. The reaction was acid-quenched and immediately injected into the mass spectrometer for analysis. All experiments were performed in duplicate. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint PLIMSTEX experiments were conducted on a Waters SELECT Series CyclicIMS system coupled to two I- Class UPLC pumps (Waters). The separation gradient was 5-35% acetonitrile over 3 minutes at a 100 μL/min flow rate. The mass spectrometer was calibrated using the Major Mix (Waters) and operated with the following parameters: capillary voltage 2.8 kV, trap collision energy 4 V, sampling cone 30 V, source temperature 80°C, and desolvation temperature 175°C. For the PLIMSTEX data analysis of AL LC titration with M83, the peptide fragment 101NWVFGGGTKL110 (numbered according to the sequence alignment, equivalent to residues 98-107 of the AL LC sequence) was selected. This peptide was chosen because it contains residues that form the stabilizer binding site in WIL-FL, notably F104 (Morgan et al. 2019). Accordingly, it exhibited one of the strongest responses to kinetic stabilizer binding. Size exclusion chromatography Protein (AL VL, 0.24 mg/mL, 20 μM) was incubated for 30 minutes at 37°C in the presence or absence of M83 (100 μM) in PBS, pH 7.4, containing 1 % (v/v) DMSO. Following incubation, the protein mixture was loaded onto a Superdex® 75 10/300 column (Cytiva) equilibrated with PBS, pH 7.4, and eluted using an AKTA Pure FPLC system (Cytiva) at a flow rate of 0.5 mL/min, while monitoring the absorbance at 280 nm. M83 was added at a 1:5 (mol:mol) ratio. The column was calibrated using protein standards (Sigma): blue dextran (2000 kDa), bovine serum albiumin (66 kDa), carbonic anhydrase (29 kDa), cytochrome C (12.4 kDa), and aprotinin (6.5 kDa). Limited proteolysis LCs (0.2 mg/mL, ~8.3 µM) were incubated in PBS, pH 7.4, containing 1% DMSO at 37°C with agitation at 450 rpm in the presence or absence of 100 µM of M83. Proteolysis was initiated by adding trypsin (Promega, 0.5 mg/mL stock concentration, ~20.8 uM). At designated time intervals, aliquots (10 µg) of each proteolysis mixture were quenched with 0.2 % v/v formic acid and separated by denaturing electrophoresis on 10-20% acrylamide gradient Tris-Glycine gels under reducing conditions, followed by Coomassie staining. Intact LCs was quantified by densitometric analysis of the gel bands (Gel Analyzer v23.1, Istvan Lazar Jr. and Istvan Lazar Sr., available at www.gelanalyzer.com). Residual LC fractions were calculated for each time point. Proteolysis kinetics were measured over 24 h. Proteolysis rates were calculated by fitting the data to a single exponential decay, and areas under the curve (AUC) calculated using a trapezoidal method. These data were used to optimize a single timepoint experiment to determine the maximum protection afforded by kinetic stabilizer binding. Enzyme to substrate (E:S) .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint ratios ranged from 1:16 to 1:64 (w:w) and incubation times from 5 hours to 24 hours, depending on the inherent proteolytic susceptibility of each LC variant.

Structural dynamics vary among different full-length light chains We investigated seven FL λ LC proteins whose sequences were originally identified in patients with AL amyloidosis, along with two FL λ LC control sequences (Figure 1, Table 1). These sequences are derived from germline genes which are over-represented in AL amyloidosis compared to the normal repertoire (Morgan et al. 2025; Kourelis et al. 2017). As in our prior study (Peterle et al. 2021), our controls were two non-amyloidogenic λ LCs: MM, originally identified in a patient with multiple myeloma but without amyloid deposition; and GL, the protein with the precursor germline sequence from which the AL and MM sequences are derived, IGLV6-57. To identify APRs within the FL LC sequences we used the AmylPred2 server (Tsolis et al. 2013), which combines the results of multiple algorithms, producing a consensus score from 0 to 10. Similar regions of sequences were identified in each FL LC, although the strength of the predictions varied between sequences (Figure 2A). VL domains harbored two (H6) to six (GL, MM, H16 and MCG) APRs (AmylPred2 score > 5). Two segments in the CL domain, common to all nine FL LCs, were also predicted as APRs. These segments predominantly form ß-strands within the native LC structure (Figure 2A) but may drive self-association upon local or global unfolding. We first employed HDX-MS to investigate the local backbone conformational dynamics of FL LCs under identical conditions in the absence of kinetic stabilizer small molecules. HDX-MS provides detailed insights into solvent exposure and hydrogen bond stability by monitoring the exchange of backbone amide hydrogens with deuterons in the solvent (Konermann, Pan, and Liu 2011). The exchange was initiated under native-like conditions where the protein was folded. Greater deuterium incorporation reflected greater conformational dynamics and/or solvent exposure. Exchange was quenched at specific timepoints, from 10 sec to 16 h, by denaturation of the protein at acidic pH, where the average intrinsic rate of backbone amide HDX is minimal, followed by peptic digestion to generate peptides for LC-MS analysis. The extent of exchange at different time points was determined by measuring deuterium incorporation relative to that of the undeuterated protein, and was normalized relative to the experimental maximal deuterium uptake (maxD) observed for each peptide, as previously described (Peterle, Wales, and Engen 2022). For each LC, sequence coverage exceeded 95% (Figure S2). .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint To facilitate comparisons among different isoforms, HDX-MS results were visualized as skyline plots, which show percent deuteration at each residue interpolated from peptide-level exchange data. Figure 2B shows the data for 1 minute of exchange and Figure S3 shows other timepoints. No systemic differences between FL LCs with a histidine tag (AL, MM and GL) compared to other (untagged) FL LCs were observed by HDX (Figure 2B and S3). Figure 2C compares deuterium uptake kinetics for representative peptides in specific regions of interest, including CDR1, CDR2, CDR3, and the residue segment 133-139 from CL. The latter segment was selected because it partially overlaps with the amyloidogenic region 136-145 and encompasses a known proteolytic hotspot whose cleavage can generate a VL-containing LC fragment found in human amyloid deposits (Lavatelli et al. 2020; Mazzini et al. 2022; Lavatelli et al. 2024). We observed large variations in HDX within and between the FL LCs, mainly in the VL domains, reflecting their variable sequences. As expected, the solvent-exposed CDR loops exhibit more deuteration, corresponding to the low structural protection of amides from HDX, as compared to the FRs, which contain more hydrogen-bonded β-sheets. The deuteration level in each region varied among different LCs. The least protected regions were adjacent to the APRs identified by AmylPred2. However, portions of these APRs showed low exchange indicating high protection by the native LC structure. This included high protection in C21 and C140 that are located in amyloidogenic segments and form internal disulfides in the VL and CL domains, respectively. The counterpart cysteine residues in the intermolecular disulfide bonds, C92 and C200, respectively, are located in regions of variable solvent exposure: C92 resides in a relatively exposed area near CDR3, whereas C200 is positioned within a more protected region. As expected, the extent of C L deuterium incorporation is similar for the nine LCs studied, reflecting the sequence and structural conservation of CL. Most differences in HDX were observed in the first 20 residues of CL which are adjacent to the VL domain. Within these residues, segments from AL, MM, GL, H3 and H16 showed lower structural protection (greater exchange) after 1 minute than those of H6, H7, H9 and MCG. These differences may be associated with differential interactions between the two domains. Overall, no clear and strict correlation was identified between the observed deuteration levels in specific regions and the amyloid-forming properties of the LCs under study. However, compared to the non- amyloidogenic isoforms GL and MM, which share a very similar HDX profile, all amyloidogenic counterparts showed lower protection in the V L domain, but not in the CL domain. AL, H3, H9, and H16 exhibited generally rapid exchange across the entire VL, particularly in the CDRs. MCG showed greater .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint deprotection in CDR1 and CDR3 at shorter time points, while FR3 exchanged to a greater extent at longer time points. H6 and H7 were more difficult to compare due to differences in peptide lengths and positions, but they exhibited increased uptake in FR4, FR1, and FR3 while remaining more protected in CDR1 and CDR2. Stabilizer binding reduces FL AL LC deuterium incorporation We next investigated the effects of stabilizer molecules on deuterium uptake of AL LC. HDX-MS was carried out using 1.5 µM AL LC in the presence of 15 µM stabilizer. These concentrations are comparable with the circulating concentrations of free LCs (Katzmann et al. 2002) and an approved kinetic stabilizer drug for transthyretin amyloidosis (Cho et al. 2015). Figure 3A shows differences in normalized deuterium uptake of AL LC peptic peptides in the presence of P1, P5, B20, M53, M63 and M83, compared with the vehicle control (0.15% v/v DMSO), presented as peptide-level heatmaps (“chiclet plots”) across all labeling times. For clarity, only peptides from the VL domain are shown; complete data are shown in Figure S4. Example data for the peptide covering residues 101–110 (101NWVFGGGTKL110, numbered according to the sequence alignment in Figure 1, corresponding to sequential positions 98– 107 of AL LC) is shown in Figure 3B. This peptide comprises residues in CDR3 and FR4 and also forms part of the VL-VL interface. No differences were detected at short labeling times; at longer times, increased stabilizer-induced protection from HDX was detected for four out of six stabilizer molecules (M83, B20, M53, P1). The region with the greatest change in protection from HDX was residues 92–110 (equivalent to sequential positions 89–107), which extends from C92 of the intra-domain disulfide bond through CDR3 to FR4. An additional site exhibiting less increased protection from HDX was observed between residues 34 and 48 (Figure 3A). Only minor stabilizer-induced changes were detected in CL domain, which were most evident for residues 165-180 in the presence of M83 (Figure S4). Stabilizer molecules P5 and M63 did not alter deuterium uptake. The other four stabilizers resulted in increased protection from HDX in the order M83>B20>M53>P1. This is the same order as the small-molecules’ efficacy determined in the assay that was originally used for drug optimization, which measured protection of the WIL-FL LC from endoproteolysis (Morgan et al. 2019; Yan et al. 2021). Similar residues were protected from exchange by all four kinetic stabilizers. To determine the relative efficacy of the small-molecule stabilizers, we measured deuterium uptake by AL LC (0.25 µM) as a function of stabilizer concentration. M83, B20, M53, and P1 were titrated from 0.2 to 25 µM. We analyzed the data using the PLIMSTEX approach (Protein Ligand Interaction by Mass Spectrometry, Titration, and EXchange) (Zhu et al. 2003; Zhu, Rempel, and Gross 2004). In a PLIMSTEX .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint experiment the labeling time is fixed, and protein-ligand interaction is monitored through changes in deuterium incorporation across a titration series of the ligand. AL LC peptide 101NWVFGGGTKL110, described above, was selected for PLIMSTEX analysis. This peptide exhibits a large change in deuterium uptake upon stabilizer binding. The analysis was conducted at a labeling time of 1 hour and 30 minutes, chosen to capture the maximum observable protection from exchange while allowing the system to approach the near steady-state equilibrium of the exchangeable hydrogens (Zhu, Rempel, and Gross 2004). PLIMSTEX analysis of the HDX data indicated that M83 decreases deuterium uptake at concentrations 100-fold lower than that of the other stabilizer molecules (Figure 3C). We chose to focus the remainder of our studies on M83, the most efficacious stabilizer, in order to investigate the mechanism by which M83 protects AL LC from exchange. We used two additional forms of the AL protein: AL LC C218S, which cannot form the intermolecular disulfide linking the CL domains; and AL VL, the stand-alone VL domain. Both these proteins equilibrate between monomer and non- covalent dimer in solution. At the concentrations used in HDX-MS, AL C218S is primarily dimeric and AL VL is primarily monomeric (Peterle et al. 2021). Figures 4A–4C show HDX-MS data from AL LC, AL C218S and AL VL, respectively, in the presence or absence of M83. Consistent with our previous studies, unliganded AL LC exhibited greater protection from HDX than AL C218S or AL VL (difference heatmaps in the right-most columns of Figures 4B and 4C). These data are consistent with progressive stabilization associated with the presence of the CL domain and intramolecular disulfide bond that has been observed in other FL LCs (Peterle et al. 2021; Klimtchuk et al. 2023; Rennella et al. 2019; Puri, Gadda, et al. 2025). Figure S5 shows the same data as peptide- level chiclet plots. Binding of the stabilizer molecule led to a large decrease in deuteration (i.e., an increase in HDX protection) observed from middle to long exchange times. For VL, this change in deuteration was no longer apparent at 16 hours, likely because both bound and unbound states of the protein had reached equilibrium with the solvent. Notably, this increased protection from HDX was observed in similar V L segments of all three protein constructs. These segments were also more protected in AL LC than in AL C218S or AL VL, indicating that stabilizer binding mimics the effect of increased dimer formation that was previously observed for these proteins (Peterle et al. 2021). Unlike VL, the CL domain showed only a small increase in protection upon stabilizer binding to FL LCs, mainly in residues 165–180, which are also more protected in AL LC than in AL C218S. The observed deuterium incorporation was only slightly reduced in M83-bound AL LC compared to M83-bound AL C218S. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Accordingly, the change in deuterium incorporation upon M83 binding observed for AL C218S was greater than that observed for AL LC. We mapped the differences in AL LC deuteration in the presence and absence of M83 onto an AlphaFold3 model of AL LC, since no experimental structure of this FL LC is available (Figure 4D). Multiple backbone regions exhibited increased protection from HDX in the presence of M83. The greatest increase in protection was observed in peptides that form the VL-VL interface. Altered exchange in this region is consistent with M83 binding in a similar site to that observed for other stabilizer molecules in co-crystal structures with LCs (Morgan et al. 2019; Yan et al. 2020, 2021; Yan, Wilson, and Kelly 2023; Lederberg et al. 2024). In addition, residues from the solvent-exposed ß-strands CV, C’V, FV and HV, of the VL domain also show increased protection upon M83 binding. CL residues 165–180, which show a small increase in protection upon stabilizer binding, form the CL-CL interface and are located close to the CL-VL domain interface. Kinetic stabilizer binding enhances self-association of VL domains To further investigate the interaction between stabilizer binding, dimerization and HDX, we applied the PLIMSTEX approach, as above, to measure the apparent affinity of M83 for the three AL constructs. We asked whether binding of M83 could force AL C218S and AL VL to form a dimeric molecule with protection from HDX equivalent to that of the unbound or bound disulfide-linked dimer. M83 was titrated against each AL construct and the deuterium incorporation measured after 90 minutes. Raw mass spectra of peptide 101NWVFGGGTKL110 at varying concentrations of M83 are presented in Figure 5A, and the averaged centroid values of the spectra plotted against concentration of M83 are shown in Figure 5B. Without M83, deuterium incorporation for peptide 101NWVFGGGTKL110 differed significantly among the three AL constructs, reflecting differences in their intrinsic stabilities shown, consistent with previous experiments (Peterle et al. 2021). AL VL exhibited the highest deuterium uptake (D0 = 6.34 Da, Figure 5A), AL C218S showed intermediate uptake (D0 = 5.20 Da), and AL LC showed the lowest uptake (D0 = 3.73 Da). M83 titration resulted in a concentration-dependent reduction in deuterium uptake across all three protein constructs, confirming specific binding. The maximum reduction in deuterium incorporation (ΔD, measured between the centroids of the m/z distributions) was observed at 25 µM M83, the highest stabilizer concentration investigated and 100-fold in excess of protein. The ΔD values for AL LC, AL C218S and AL VL were -1.37 Da, -2.85 Da and 2.61, respectively. The change in deuteration was greater for the non-covalent constructs than for AL LC upon M83 binding. However, this quantitative analysis showed that neither AL C218S nor AL VL reached the same protection from .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint exchange as M83-bound AL LC. M83 binding was sufficient to reduce uptake of deuterium by AL C218S, but not AL VL, to below the level measured for unliganded AL LC. Fitting the observed ΔD to a unimolar binding model (1:1 LC dimer:ligand) yielded protection midpoints (EC50, the concentration of 50% maximal effect) of 0.65 μM for AL LC, 1.8 μM for AL C214S and 2.2 μM for AL VL (Figure 5C; reported values are the mean of two independent measurements). These values are not directly comparable because the dimerization equilibria and exchange endpoints are different for the three AL constructs and hence, these values should not be treated as dissociation constants. The distributions of discrete m/z states observed in each experiment for peptide 101NWVFGGGTKL110 report on the ensembles of species within the exchange reaction, averaged over the 90-minute timecourse. AL LC spectra had similar distributions of peaks at all concentrations of M83, consistent with homogeneous exchange. The spectra of AL C218S and AL VL were more complex, indicating the presence of multiple populations of exchanged species. Unliganded AL C218S had a broad distribution of states that becomes narrower as the concentration of M83 increases. AL VL exhibited different behavior, where increasing M83 led to the appearance of a population with less incorporation of deuterium. We hypothesize that this behavior reflects ligand-induced dimerization of both non-covalent species. Under the maximum concentration of M83 tested, only a sub-population of AL VL is stabilized. We next asked whether kinetic stabilizer binding could enhance VL domain dimerization. M83 increases the equilibrium population of VL dimer, as determined by analytical size exclusion chromatography (Figure 5C). This observation is consistent with drug binding in the VL-VL interfacial cavity, and with the previous observation that P1 binding favors dimerization of WIL-FL C218S (Morgan et al. 2019). Stabilizer molecules reduce hydrogen exchange and endoproteolysis of diverse LCs We next asked whether binding of M83 alters the stability and dynamics of other FL LCs. We measured HDX kinetics for each FL LC (1.5 µM) in the presence and absence of 15 µM M83. Figure 6A shows the difference in deuteration between FL LCs with and without M83 as residue-level heatmaps, while Figure 6B shows the data mapped onto the dimeric VL domains of structural models. All FL LCs exhibited reduced deuteration in the presence of M83, particularly between 1 to 4 hours of exchange (further data are provided in Figures S6 and S7). The protein segments showing the most significant stabilizer- induced protection from HDX were consistent across eight of the nine proteins, with the strongest effects observed in FR4 and, in some cases, CDR3. An exception was H6, which exhibited increased .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint protection primarily within FR2. Only AL LC and GL LC exhibited increased protection within the CL domain. To further assess the structural impact of M83, we conducted limited proteolysis experiments using trypsin at neutral pH on FL LCs in the presence or absence of M83 (Figure 7). We initially measured timecourses for each FL LC under identical conditions, with timepoints ranging from 1 minute to 24 hours (Figure 7A and Figure S8). Although we were able to fit data for some FL LCs to exponential decay models (Figure 7A–B and Figure S8), this was not successful for all FL LCs. Therefore we calculated the area under the curve (AUC) for these data to define a simple metric for protease sensitivity (Figure 7A and Figure S8). For comparison, we calculated an equivalent AUC for HDX data (Figure 7B and Figure S8). Since the intrinsic proteolysis rates and the magnitude of M83-induced protection varied across the FL LCs, we tailored single timepoint proteolysis experiments by selecting optimized conditions for each FL LC (Figure 7D). The protease sensitivity of the FL LCs and the effect of M83 varied substantially. There was only a weak correlation between the intrinsic protease resistance of each FL LC and its protection from HDX (Pearson’s correlation coefficient R = 0.14, Figure 7E). Furthermore, the extent of protection from protease and HDX were weakly correlated, both when comparing the AUC for the proteolysis timecourses (R = -0.3, Figure 7F) and the optimized, single timepoint data (R = 0 069, Figure 7G). These observations indicate that limited trypsin proteolysis and HDX measure different aspects of stability, likely due to differential cleavage of unstructured peptide bonds within the folded states. However, both

demonstrated stabilization of all FL LCs upon binding to M83.

This work demonstrates the ability of small-molecule kinetic stabilizers to bind to multiple LCs and thereby suppress their dynamics and proteolytic susceptibility. LC dynamics, including local and global unfolding, enable self-association of non-native LCs to form amyloid, as well as proteolytic cleavage that yields more amyloidogenic VL-containing LC fragments. Binding of the most potent small molecule, M83, leads to a reduction in exchange of amide hydrogens with the solvent and decreased susceptibility to proteolytic cleavage for all nine LCs studied (Figures 6 and 7), despite their distinct sequences and dynamics (Figure 2). These data are consistent with the previous observation that small molecule binding stabilizes WIL-FL, the IGLV6-57-derived LC that was used for the high throughput screen and hit optimization to generate M83. The precursor germline genes represented by the LCs studied here, IGLV1-44, IGLV1-51, IGLV2-8, IGLV2-14 and IGLV6-57 together account for 386/847 (46%) of all amyloidogenic LCs and 386/621 (62%) of amyloidogenic λ LCs in the AL-Base repository (Morgan et al. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint 2025). By demonstrating that M83 stabilizes several LCs derived from the most commonly observed λ LC genes, our results support the hypothesis that pharmacologic stabilization of LCs is a promising therapeutic strategy that could complement existing and emerging approaches. Consistent with our previous studies (Rennella et al. 2019; Peterle et al. 2021; Klimtchuk et al. 2023, 2024) and those of other groups (Puri, Gadda, et al. 2025; Weber et al. 2020; Rottenaicher et al. 2021; Puri, Palkar, et al. 2025), the extent of amide exchange varies across the sequence of the LCs. The VL domains of the seven amyloidogenic proteins have distinct patterns of deuterium uptake. There are no clear patterns that could represent a “signature” of amyloid propensity other than our previous observations that AL LC is less protected from exchange than the non-amyloidogenic IGLV6-57-derived MM LC or GL LC. None of the LCs investigated here exhibited increased exchange in the C V and CV’ strands (residues 38-49) that were identified as rapidly exchanging in the amyloidogenic IGLV6-57- derived LC AL55 which may be related to the altered VL–VL interface observed for this specific LC (Puri, Gadda, et al. 2025). Instead, we observed more rapid HDX in the region encompassing CDR2 and strand DV (Figure 2). In contrast, similar patterns of deuterium uptake were observed in all nine CL domains, consistent with their similar sequences and structures. CL domain mutations have been associated with instability and amyloid formation (Benson, Liepnieks, and Kluve-Beckerman 2015; Rottenaicher et al. 2023; Rennella et al. 2019), but our data suggest that in the absence of such mutations, the dynamics of the unmutated CL sequences are indistinguishable within free LC dimers. Overall, these results and our previous study of κ LCs (Klimtchuk et al. 2023) are consistent with the hypothesis that multiple types of sequence and structural changes can lead to amyloidogenic LCs. We asked whether stabilizer binding would lead to similar structural changes in LCs with different local dynamics. The stabilization imparted to all tested LCs is consistent with similar modes of binding between LCs, as observed in co-crystal structures of stabilizers with MM and H9 (Yan et al. 2021; Lederberg et al. 2024; Yan, Wilson, and Kelly 2023). However, our analysis only measures the effect of stabilizer binding on HDX and cannot directly report on the conformation of the LC or small molecule. It is possible that M83 can bind in different conformations to that observed for other stabilizers and LCs, particularly in the case of H6, which has a different pattern of differentially-protected regions than the other LCs (Figure 6). We hypothesize that stabilizer binding enhances structural coupling between the constituent domains of a full-length LC dimer (Rennella et al. 2019), so that both global and local structural fluctuations are reduced. In agreement with this idea, stabilizer binding enhances dimerization and increases protection .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint in both the residues that define the binding pocket and residues forming the dimeric interface, such as strand A, FR2, strands E and F, CDR3 and J-region of the VL domain as well as strand E of the CL domain (Figures 4–6). On the other hand, relatively little change in protection was observed for the most labile protons in the loops of CDR1 and CDR2, indicating that these residues do not form new hydrogen bonds. However, the global protection from protease digestion afforded by stabilizer binding indicates that these mobile regions are not susceptible to trypsin proteolysis without local or global unfolding. Importantly, M83 binding increased local protection in CDR3 and FR4 regions in all proteins but H6 (Fig. 6A). CDR3 is adjacent to C92 that forms an internal disulfide (C21–C92) in V L. The structure around this conserved disulfide must fully unfold to enable the relative backbone rotation by 180 degrees, from parallel in native V L to antiparallel in amyloid (Radamaker et al. 2019). This backbone rotation likely provides a major contribution to the kinetic barrier for LC misfolding in amyloid; if so, suppression of local backbone dynamics in the regions adjacent to the C21–C92 disulfide, particularly the highly dynamic CDR1 and CDR3, is expected to decelerate amyloid formation (Klimtchuk et al. 2023). Therefore, M83-induced stabilization of CDR3 and adjacent regions in most LCs explored suggests M83 should suppress LC amyloid formation. The largest reduction in deuterium uptake induced by M83 was observed for AL LC (Figure 6A). Other amyloidogenic LCs showed a reduced level of stabilization, which may be due to the optimization of stabilizers for binding to IGLV6-57-derived LCs. The reduced protection afforded to GL LC and MM LC by stabilizer binding appears to be due to their increased stability in the absence of the small molecule. Binding of M83 is not sufficient to globally reduce the level of exchange of AL LC to that of the non- amyloidogenic LCs (Figure 6 and Figures S5–S6). However, the stabilization of AL LC’s structured regions by M83 reduced their exchange to a level similar to that observed for equivalent regions of unbound GL LC. The M83-bound states of AL LC and AL C218S exhibited similar exchange kinetics (Figure 4A and 5), where the M83-bound state of AL C218S was slightly less stable than M83-bound AL LC but more stable than unbound AL LC. We therefore suggest that stabilizer binding can compensate for the loss of stability associated with reduction of the intermolecular disulfide bond, and that the effect of stabilizers will not be limited to disulfide-linked dimers in patients. The major limitation of our study is that these nine LCs represent only a fraction of the vast potential diversity of light chains. Although we expect that the stabilizer can bind to most λ LCs, it is not clear how much stabilization will be imparted in each case and whether this will be sufficient for clinical efficacy. Coumarin-based stabilizers including M83 bind relatively weakly to κ LCs (Morgan et al. 2019; Yan et al. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint 2021), which account for approximately 20% of AL amyloidosis clones (Morgan et al. 2025). Furthermore, it is not clear how the dynamics that are measured by HDX relate to amyloid propensity, since there is no clear correlation between the patterns of exchange protection observed for each LC and its pathogenicity. Our data will support further work to identify such mechanistic details. Stabilization of LCs is a novel and potentially valuable therapeutic approach that could complement existing therapies. This work demonstrates that kinetic stabilizers can bind to multiple LCs and reduce the conformational dynamics associated with proteolysis and aggregation, which is essential for their broader utility. In combination with our previous work developing stabilizers with increased affinity (Yan et al. 2021) and specificity for LCs in blood (Lederberg et al. 2024), the current study supports further development of these molecules as therapeutic candidates.

This work was supported by National Institute of Health Awards R01-GM067260, R01-GM135158 and R01-HL157566; the Wildflower Foundation; and the Boston University Amyloid Research Fund. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figures and legends .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure 1: Kinetic stabilizers to inhibit aggregation of diverse antibody light chains. (A) Schematic representation of systemic AL amyloidosis pathogenesis and the mechanism of action of kinetic stabilizers. Unstable LCs are overexpressed by abnormal proliferating plasma cells and released into the bloodstream as homodimers, composed of a variable V L domain (in yellow) and a constant CL domain (in gray). An inter-molecular disulfide bond between cysteine residues at position 218 is observed in some LCs. Each clone produces a unique LC sequence. LCs can undergo unfolding, oligomerization, and proteolysis events, eventually leading to formation of fibrils that accumulate in various organs, most frequently the heart and kidney, resulting in progressive organ damage. Proteolysis can release aggregation-prone fragments that may act as templates or seeds for intact LCs. Kinetic stabilizers prevent fibril formation by stabilizing the dimeric native structure, thus reducing the concentration of aggregation-competent species. (B) Sequence logo plot of 554 V L domains of λ LCs taken from AL-Base. The height of each letter is proportional to its frequency in the alignment and the overall height of the column is proportional to the information content at that position. Amino acids interacting with kinetic stabilizers are indicated according to the numbering used in the original crystal structure (PDB code 6MG5) and color-coded according to the substructure of the M83 stabilizer to which they bind (see the structure of M83 in panel (D): red, anchor substructure; blue, aromatic core; green, linker module; purple, distal substructure). (C) Multiple sequence alignment of the 9 selected LCs explored in this study. The shading indicates the degree of conservation of amino acid residues. V L domain framework regions (FR1–4) and complementarity determining regions (CDR1–3) are shown in green and yellow, respectively. Blue and red boxes show the locations of the native secondary structure elements. Individual ß-strands are labeled. Intramolecular disulfide bonds are shown by orange lines. Note that the IMGT regions are defined to allow comparison between different immunoglobulin domains and do not correspond precisely to LC secondary structure elements. (D) Structures of the kinetic stabilizers used in this study. M83, the stabilizer molecule that showed the highest potency in LC stabilization, has its substructures highlighted. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure 2: Hydrogen-deuterium exchange profiles of LCs. (A) Sequence alignment of the nine LCs under study, highlighting in purple the residues with amyloidogenic propensity as predicted by the AmylPred2 webserver. The shading represents the number of algorithms within AmylPred2 that identified each residue as amyloidogenic. (B) Skyline plot showing the percent of deuterium incorporation (%D) across the aligned LC amino acid sequences at 1-minute labeling time point. Gray shading represents CDRs 1, 2 and 3 within V L and residues 133-139 within CL. Top, middle, and bottom panels correspond to LCs derived from variable gene families IGLV6, IGLV1 and IGLV2, respectively. Dashed lines show the .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint boundary between the variable and constant domains. The secondary structure scheme is shown at the top of the panels, with blue boxes representing ß-sheets and red indicating α-helices. Intramolecular disulfide bonds are shown by orange lines. (C) Deuterium uptake plots (%D) are shown for specific peptides covering regions of interest, including CDR1, CDR2, CDR3, and the constant region (CL). Each line corresponds to a specific LC variant, with peptide sequence numbers indicated. Note that these plots are not directly comparable due to sequence differences between the peptides. Complete HDX-MS

for all proteins and labeling times are reported in Figures S3, S6 and S7. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure 3: Differential stabilization of 1.5 µM AL LC by six small molecule stabilizers. (A) Peptide-level chiclet plot of deuterium uptake of FL AL LC in the presence or absence of 15 µM kinetic stabilizers. Only peptides originating from the VL domain are shown; complete data are provided in Figure S4. “N” and “C” indicate the N- and C-termini, respectively, of the peptic peptides, numbered according to the sequence of AL LC. The AL LC peptide 101NWVFGGGTKL110 (corresponding to sequential positions 98-107) is highlighted with a red arrow. Vehicle (Veh) represents DMSO at 0.15% v/v during exchange. (B) Deuterium uptake curves for peptide 101NWVFGGGTKL110. (C) PLIMSTEX curves for peptide 101NWVFGGGTKL110 titrated with P1 (blue), B20 (green), M53 (magenta), and M83 (red) are shown as a function of the stabilizer molecule concentration. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure 4: Effects of the kinetic stabilizer M83 binding to AL constructs monitored by HDX-MS. Residue- level heatmaps display percent deuterium incorporation (%D) for the proteins in the presence or absence of M83, as well as the corresponding differences in deuterium uptake (Δ%D). “Veh” represents .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint DMSO vehicle at 0.15% v/v during exchange. Horizontal lines indicate the boundaries between the variable (VL) and constant (CL) domains. (A) AL LC. (B) AL C218S. (C) AL VL. Peptide-level data are provided in the Figure S5. Differences between constructs in the absence of M83 (C218S – LC and VL – LC) are also shown. The protection induced by the kinetic stabilizer is greatest at peptides corresponding to the dimeric interface regions, but is not restricted to these residues. (D) Change in deuteration (Δ%D [(AL LC + M83) - AL LC]) after 1 hour of labeling mapped onto an AlphaFold 3 model of the AL LC dimeric structure. Regions of increased protection are shown in shades of blue. The names of the β-strands within the V L domain are shown for one monomer. Figure 5: Stabilizer binding promotes LC dimerization. (A) Raw mass spectra of peptide 101NWVFGGGTKL110 from AL LC, AL C218S, and AL VL in the presence of varying concentrations of M83 at a single time point of 90 minutes. Proteins concentration was 0.25 µM monomer equivalent. The blue peaks represent the isotopic distribution of the peptide, with centroid shifts from the undeuterated state indicating the average extent of deuterium incorporation (ΔD) (B) PLIMSTEX titration data for peptide 101NWVFGGGTKL110 from AL LC (red), AL C218S (black), and AL VL (teal), showing measured .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint deuterium uptake values (average of duplicates, where error bars show the range of the measurements) with corresponding fitted curves. (C) Size exclusion chromatography (SEC) of AL VL in the absence (black) and presence (red) of 100 µM M83, illustrating its effect on dimer formation. M and D labels refer to the elution volume of the peaks corresponding to the monomeric and dimeric form of VL. Peaks corresponding to molecular weight standards are shown above. Figure 6: Effect of M83 binding on multiple LC proteins monitored by HDX-MS. (A) Single-residue aligned heatmaps of percent deuterium difference (Δ%D) across the nine LCs. The solid horizontal line indicates the boundary between the VL and CL. Protection from deuterium exchange is observed for all LCs upon incubation with M83. Complete data are provided in Figure S6 and S7. (B) Structural mapping of Δ%D onto VL dimer structures for each isoform highlights regions of stabilization upon M83 binding after 1 hour of exchange. The relative orientation of the VL and CL domains differs between the models, so for clarity only VL is shown. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure 7: Effect of M83 binding on multiple LC proteins monitored by limited proteolysis. (A) Kinetics of digestion of H16 LC by trypsin in the presence (red) or absence (black) of M83, analyzed by SDS-PAGE. Data were analyzed by fitting to a single-exponential decay and by calculating the area under the curve (AUC). Data for other LCs are provided in Figure S8. (C) Proteolysis rates from fits of timecourse data to single exponential models. Hollow symbols and bars represent rates and fitting errors for successful fits (see Figure S8), solid symbols show data for which no rate could be determined. (B) AUC analysis of H16 HDX in the presence and absence of M83 for comparison with (A). (D) Single point proteolysis using optimized conditions to determine the maximal protection from protease afforded by M83 binding. Quantitation of the data is shown by the bars. (E–G) Correlations between proteolysis and HDX measurements of the intrinsic LC stability or stabilization imparted by M83. The blue dashed lines indicate linear regression lines with associated Pearson correlation coefficients (R) and significance values (p). .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Table Name (alternative names) Germline variable gene Germline constant gene Sequence NCBI accession PDB code

Disease AL (AL-150L; 01-095) IGLV6-57 IGLC2 EF589390 N/A (Peterle et al. 2021) AL MCG IGLV2-8 IGLC1 3MCG_1 3MCG (Schiffer et al. 1973) AL H3 (AL30) IGLV1-44 IGLC3 KC433670 5MTL (Oberti et al. 2017) AL H6 (AL50) IGLV1-51 IGLC2 KY471433 5MUD (Oberti et al. 2017) AL H7 (AL48) IGLV1-51 IGLC3 KC433671 5MUH (Oberti et al. 2017) AL H9 (AL52) IGLV2-8 IGLC2 KY471435 5M6A (Oberti et al. 2017) AL H16 (AL54) IGLV2-14 IGLC3 KY471437 N/A (Oberti et al. 2017) AL MM (JTO) IGLV6-57 IGLC3 6MG4_A 6MG4; 1CD0 (Wall et al. 1999) MM GL (6aJL2) IGLV6-57 IGLC2 2W0K_A (VJ only) 2W0K (Peterle et al. 2021) Germline sequence Table 1: LC proteins used in the current study. Genes are defined according to the IMGT system. PDB identifiers are provided where experimental structures are available. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint

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It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Zhu, Mei M., Don L. Rempel, Zhaohui Du, and Michael L. Gross. 2003. “Quantification of Protein-Ligand Interactions by Mass Spectrometry, Titration, and H/D Exchange: PLIMSTEX.” Journal of the American Chemical Society 125 (18): 5252–53. https://doi.org/10.1021/ja029460d. Zhu, Mei M., Don L. Rempel, and Michael L. Gross. 2004. “Modeling Data from Titration, Amide H/D Exchange, and Mass Spectrometry to Obtain Protein-Ligand Binding Constants.” Journal of the American Society for Mass Spectrometry 15 (3): 388–97. https://doi.org/10.1016/j.jasms.2003.11.007. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry Daniele Peterle, Nicholas L. Yan, Elena S. Klimtchuk, Thomas E. Wales, Olga Gursky, Jeffery W. Kelly, John R. Engen, Gareth J. Morgan Supplementary Appendix Protein sequences Supplementary Figures S1-S8 .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Protein sequences >AL NFMLTQPHSVSESPGKTVTISCTRSSGSIASTYVQWYQQRPGSAPTNVIFEDNERPSGVPDRFSGSIDSSSNSAYLTISGLKTED EADYYCQSYGTNNWVFGGGTKLTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSY SCQVTHEGSTVEKTVAPTECS >GL NFMLTQPHSVSESPGKTVTISCTRSSGSIASNYVQWYQQRPGSSPTTVIYEDNQRPSGVPDRFSGSIDSSSNSASLTISGLKTED EADYYCQSYDSSNWVFGGGTKLTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSY SCQVTHEGSTVEKTVAPTECS >MM NFMLNQPHSVSESPGKTVTISCTRSSGNIDSNYVQWYQQRPGSAPITVIYEDNQRPSGVPDRFAGSIDRSSNSASLTISGLKTED EADYYCQSYDARNVVFGGGTRLTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSY SCQVTHEGSTVEKTVAPTECS >H3 QSVLTQPPSTSGTPGQRVTISCSGSSSNIETNTVNWYQQLPGTAPKLVMHTNNQRPSGVPDRFSGSRSGTSASLAIGGLQSEDEA DYFCAAWDDNLNGVIFGGGTKLTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSY SCQVTHEGSTVEKTVAPTECS >H6 QSVLTQPPSVSAAPGQKVTISCSGNNSNIGKNYVSWYQQLPGRTPKVIMYENNKRSSGIPDRFSGSKSGTSATLGITGLQTGDEA DYYCGVWDSSLSGGVFGGGTKVTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSY SCQVTHEGSTVEKTVAPTECS >H7 QSVLTQPPSVSAAPGQKVTISCSNVGKNFVSWYQQFPGTAPKVVIYDTDKRPSDIPDRFSGSKSGTSATLDITGLQTGDEADYYC GTWDSGLNGGVFGGGTKVTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSY SCQVTHEGSTVEKTVAPTECS >H9 QSALTQPPSASGSPGQSVTISCTGTSSDVGGSDSVSWYQQHPGKAPKLIIYEVSQRPSGVPNRFSGSKSGNTASLTVSGLQAEDD ADYYCSSYGGDNNLFFGGGTKVTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSY SCQVTHEGSTVEKTVAPTECS >H16 QSALTQPASVSGSPGLSITISCTGTSSDIGGYNSVSWYQQHPGKAPKLIIYEVSNRPSGISNRFSGSKSGYTASLTISGLQAEDE ADYYCSSYTNSGILFGGGTELTVL GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSY SCQVTHEGSTVEKTVAPTECS >MCG QSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDE ADYYCSSYEGSDNFVFGTGTKVTVL GQPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSY SCQVTHEGSTVEKTVAPTECS .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Supplementary Figures Figure S1. SDS-PAGE characterization of the nine full-length LCs used in this study. Proteins were run on a 10–20% acrylamide gel under reducing conditions and the gels were stained with Coomassie. 7 μg of each protein sample was loaded per lane. Molecular weight markers are indicated on the left. The secondary bands underneath the main LC band appear to be alternative conformers the main LC protein, since no truncated species were observed by mass spectrometry. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S2. Sequence coverage maps of LCs constructs used in this study. Horizontal purple bars below LC sequence indicate the peptides for which HDX was followed. Vertical lines mark the separation between the VL and the CL. The number of peptides, sequence coverage (%), and average redundancy values are reported for each LC. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint VL CL VL CL VL CL VL CL VL CL VL CL 1 min 10 min 1 hr 4 hr 16 hr .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S3. Single-residue aligned skyline plots for all light chains (LCs) at six different labeling time points: 10 seconds, 1 minute, 10 minutes, 1 hour, 4 hours, and 16 hours. Percent deuterium incorporation (%D) is plotted against amino acid number, with vertical dashed lines indicating the boundary between V L and CL domains. Gray boxes indicate the CDR regions. Each line represents a specific LC isoform, defined in the legend on the right. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S4. HDX-MS screening of six different kinetic stabilizers. Peptide chiclet plots display differences in the percent deuterium uptake across the sequence of AL LC upon binding of each compound. The compounds screened were P1, B20, M53, M83, P5, and M63. On the left, the absolute uptake of AL LC (no compound) serves as the baseline for comparison. M83 shows the most significant protection, followed by B20, M53, and P1, with decreasing levels of protection. P5 and M63 do not show notable differences in HDX. The horizontal line separates the variable (VL) and constant (CL) domains. Regions with no data (peach) or no change (gray) are indicated. The AL LC peptide 101NWVFGGGTKL110 (corresponding to sequential positions 98-107) is highlighted with a red arrow. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S5. Binding of the kinetic stabilizer M83 to AL LC, C214S, and VL monitored by HDX-MS. This figure presents the same data as Figure 3, displayed in a peptide-resolution chiclet plot format instead of residue-level heatmaps. Percent deuterium incorporation (%D) is shown for the protein in 0.15% DMSO vehicle and in the presence of M83, alongside the differences in deuterium uptake (Δ%D). Comparisons between constructs (C214S-LC and VL-LC) are also shown. Horizontal lines separate VL and CL domains. Regions with no data (peach) or no change (gray) are indicated. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 10 s 1 m 10 m 1 h 4 h 16 h 0.324 0.4595 0.6183 0.7667 0.8747 0.9163 0.3359 0.4698 0.6167 0.7599 0.8655 0.9132 0.3359 0.4698 0.6167 0.7599 0.8655 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-0.0386 -0.0191 -0.0032 -0.0215 -0.042 -0.0206 -0.0372 -0.0141 -0.0051 -0.016 -0.0315 -0.0186 -0.0372 -0.0141 -0.0051 -0.016 -0.0315 -0.0186 VL CL Nt Ct 50 100 150 200 VL CL Nt Ct 50 100 150 200 AL GL MM H3 H6 H7 H9 H16 MGC AL GL MM H3 H6 H7 H9 H16 MGC 10 sec 1 min 10 min 1 hr 4 hrs 16 hrs Time in D2O 10 sec 1 min 10 min 1 hr 4 hrs 16 hrs Time in D2O Deuterium Uptake of LC Isoforms – Percent Deuterium Uptake 15 30 45 60 75 90 100 Percent Deuterium Uptake No data 0 -25 -15 -10 -5 0 5 10 % Deuterium Difference 15 20 25 30 No data -30 -20 No change 1 2 3 C’ A B C D E F G H A B C D E F G 1 2 3 C’ A B C D E F G H A B C D E F G Effect of M83 on LC isoforms – Percent Deuterium Difference 0.3174 0.4367 0.5617 0.6695 0.7476 0.8308 0.3266 0.4515 0.579 0.6834 0.7529 0.8247 0.3266 0.4515 0.579 0.6834 0.7529 0.8247 0.3266 0.4515 0.579 0.6834 0.7529 0.8247 0.3266 0.4515 0.579 0.6834 0.7529 0.8247 0.3266 0.4515 0.579 0.6834 0.7529 0.8247 0.3266 0.4515 0.579 0.6834 0.7529 0.8247 0.3266 0.4515 0.579 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0.2428 0.3336 0.607 0.7484 0.8066 0.8897 0.2428 0.3336 0.607 0.7484 0.8066 0.8897 0.2081 0.2851 0.5104 0.6645 0.7203 0.7733 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2322 0.3024 0.501 0.6352 0.6853 0.7389 0.2502 0.3144 0.4917 0.6096 0.6547 0.7071 0.2906 0.3464 0.4919 0.5846 0.6246 0.677 0.434 0.4851 0.6075 0.6846 0.7035 0.7539 0.434 0.4851 0.6075 0.6846 0.7035 0.7539 0.434 0.4851 0.6075 0.6846 0.7035 0.7539 0.434 0.4851 0.6075 0.6846 0.7035 0.7539 0.434 0.4851 0.6075 0.6846 0.7035 0.7539 0.434 0.4851 0.6075 0.6846 0.7035 0.7539 0.4703 0.5192 0.6271 0.6949 0.7062 0.7581 0.4835 0.555 0.6568 0.715 0.732 0.7898 0.5099 0.6264 0.7161 0.7553 0.7836 0.8532 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.5723 0.6707 0.7556 0.7965 0.8396 0.9068 0.3424 0.4592 0.5931 0.7293 0.8038 0.8666 0.3509 0.4745 0.5999 0.7227 0.7957 0.8639 0.3509 0.4745 0.5999 0.7227 0.7957 0.8639 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.3549 0.4748 0.6098 0.7303 0.805 0.8669 0.4137 0.5218 0.6469 0.7623 0.8185 0.8655 0.6248 0.6902 0.7801 0.8772 0.8672 0.8608 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7312 0.7896 0.8677 0.9425 0.934 0.9346 0.7858 0.8429 0.9118 0.9681 0.9663 0.9714 0.2155 0.2495 0.3517 0.3872 0.39 0.4196 0.2156 0.2511 0.3589 0.3937 0.3984 0.4308 0.2156 0.2511 0.3589 0.3937 0.3984 0.4308 0.2156 0.2511 0.3589 0.3937 0.3984 0.4308 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2261 0.2775 0.4163 0.4665 0.4777 0.51 0.2352 0.2883 0.4303 0.4891 0.5103 0.5461 0.2313 0.2808 0.4164 0.4769 0.5048 0.5483 0.3113 0.3821 0.5557 0.6829 0.7667 0.8142 0.3256 0.3995 0.5743 0.697 0.7755 0.8195 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.338 0.4135 0.5861 0.7032 0.779 0.8202 0.2402 0.3131 0.4457 0.541 0.5949 0.6186 0.2402 0.3131 0.4457 0.541 0.5949 0.6186 0.2402 0.3131 0.4457 0.541 0.5949 0.6186 0.2402 0.3131 0.4457 0.541 0.5949 0.6186 0.2402 0.3131 0.4457 0.541 0.5949 0.6186 0.2597 0.3083 0.398 0.4801 0.537 0.5717 0.2812 0.3169 0.3876 0.4633 0.5207 0.5582 0.2726 0.297 0.3449 0.4142 0.4753 0.5206 0.2726 0.297 0.3449 0.4142 0.4753 0.5206 0.2726 0.297 0.3449 0.4142 0.4753 0.5206 0.2726 0.297 0.3449 0.4142 0.4753 0.5206 0.2523 0.2743 0.3155 0.3826 0.4405 0.4763 0.4616 0.6411 0.7386 0.765 0.7771 0.8085 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.4643 0.6325 0.7512 0.7832 0.7881 0.8267 0.3861 0.5276 0.608 0.6687 0.7164 0.7804 0.1209 0.1612 0.3125 0.4358 0.4951 0.5789 0.1493 0.1909 0.3318 0.4552 0.5204 0.6044 0.1493 0.1909 0.3318 0.4552 0.5204 0.6044 0.1493 0.1909 0.3318 0.4552 0.5204 0.6044 0.1493 0.1909 0.3318 0.4552 0.5204 0.6044 0.1493 0.1909 0.3318 0.4552 0.5204 0.6044 0.1756 0.2163 0.3332 0.4549 0.5329 0.6257 0.1756 0.2163 0.3332 0.4549 0.5329 0.6257 0.2119 0.2554 0.3654 0.4905 0.5822 0.6786 0.246 0.2933 0.402 0.5291 0.6223 0.7131 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2926 0.3455 0.45 0.5781 0.6713 0.7535 0.2979 0.3519 0.4584 0.5874 0.6794 0.7593 0.2726 0.3249 0.4377 0.5639 0.6445 0.7201 0.3582 0.4795 0.6511 0.7765 0.815 0.8497 0.3582 0.4795 0.6511 0.7765 0.815 0.8497 0.3711 0.5019 0.6798 0.8044 0.8375 0.8668 0.3822 0.5253 0.7143 0.8391 0.865 0.8877 0.3656 0.5427 0.7592 0.8967 0.9062 0.9099 0.2457 0.4135 0.6419 0.8205 0.8329 0.8351 0.223 0.3642 0.6051 0.8022 0.8136 0.8169 0.223 0.3642 0.6051 0.8022 0.8136 0.8169 0.223 0.3642 0.6051 0.8022 0.8136 0.8169 0.223 0.3642 0.6051 0.8022 0.8136 0.8169 0.223 0.3642 0.6051 0.8022 0.8136 0.8169 0.223 0.3642 0.6051 0.8022 0.8136 0.8169 0.2682 0.3207 0.4089 0.4956 0.5233 0.5985 0.3043 0.3634 0.4487 0.5338 0.5659 0.644 0.3043 0.3634 0.4487 0.5338 0.5659 0.644 0.3043 0.3634 0.4487 0.5338 0.5659 0.644 0.3585 0.4373 0.5281 0.6046 0.6396 0.7177 0.3585 0.4373 0.5281 0.6046 0.6396 0.7177 0.3585 0.4373 0.5281 0.6046 0.6396 0.7177 0.3585 0.4373 0.5281 0.6046 0.6396 0.7177 0.3585 0.4373 0.5281 0.6046 0.6396 0.7177 0.3654 0.4179 0.4894 0.5679 0.5988 0.6586 0.3637 0.4608 0.5805 0.686 0.7264 0.7624 0.3625 0.4904 0.6435 0.7675 0.8146 0.8341 0.3625 0.4904 0.6435 0.7675 0.8146 0.8341 0.3625 0.4904 0.6435 0.7675 0.8146 0.8341 0.3625 0.4904 0.6435 0.7675 0.8146 0.8341 0.3625 0.4904 0.6435 0.7675 0.8146 0.8341 0.3625 0.4904 0.6435 0.7675 0.8146 0.8341 0.4598 0.5939 0.7614 0.8727 0.8956 0.9109 0.4598 0.5939 0.7614 0.8727 0.8956 0.9109 0.4598 0.5939 0.7614 0.8727 0.8956 0.9109 0.4598 0.5939 0.7614 0.8727 0.8956 0.9109 0.4598 0.5939 0.7614 0.8727 0.8956 0.9109 0.4598 0.5939 0.7614 0.8727 0.8956 0.9109 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.3122 0.4113 0.5319 0.6495 0.7149 0.7543 0.2241 0.3371 0.579 0.7239 0.7524 0.8051 0.2371 0.3411 0.6143 0.7596 0.7988 0.8663 0.2354 0.3385 0.6116 0.7588 0.795 0.8563 0.2354 0.3385 0.6116 0.7588 0.795 0.8563 0.2221 0.3231 0.5963 0.7484 0.7857 0.8461 0.2221 0.3231 0.5963 0.7484 0.7857 0.8461 0.2074 0.307 0.5721 0.7359 0.766 0.8113 0.2034 0.3008 0.5464 0.6991 0.7243 0.763 0.2034 0.3008 0.5464 0.6991 0.7243 0.763 0.2034 0.3008 0.5464 0.6991 0.7243 0.763 0.2034 0.3008 0.5464 0.6991 0.7243 0.763 0.2034 0.3008 0.5464 0.6991 0.7243 0.763 0.2034 0.3008 0.5464 0.6991 0.7243 0.763 0.2012 0.2949 0.5295 0.6762 0.6968 0.7337 0.2012 0.2949 0.5295 0.6762 0.6968 0.7337 0.2002 0.2891 0.5091 0.6516 0.6713 0.7013 0.2094 0.2897 0.5079 0.6656 0.6986 0.747 0.3946 0.4908 0.6216 0.7204 0.7478 0.8087 0.3946 0.4908 0.6216 0.7204 0.7478 0.8087 0.4676 0.5678 0.665 0.7393 0.7618 0.8251 0.4676 0.5678 0.665 0.7393 0.7618 0.8251 0.4676 0.5678 0.665 0.7393 0.7618 0.8251 0.4676 0.5678 0.665 0.7393 0.7618 0.8251 0.5027 0.6075 0.6873 0.7508 0.7741 0.8417 0.5047 0.6195 0.6993 0.7609 0.7909 0.8563 0.442 0.578 0.6711 0.7321 0.7789 0.8481 0.513 0.6342 0.7216 0.7846 0.8381 0.9009 0.513 0.6342 0.7216 0.7846 0.8381 0.9009 0.513 0.6342 0.7216 0.7846 0.8381 0.9009 0.5523 0.6642 0.75 0.8164 0.8682 0.9242 0.5523 0.6642 0.75 0.8164 0.8682 0.9242 0.5523 0.6642 0.75 0.8164 0.8682 0.9242 0.5523 0.6642 0.75 0.8164 0.8682 0.9242 1 2 3 C’ A B C D E F G H A B C D E F G AL GL MM H3 H6 H7 H9 H16 MGC Deuterium Uptake of LC Isoforms + M83 – Percent Deuterium Uptake VL CL 10 sec 1 min 10 min 1 hr 4 hrs 16 hrs Time in D2O Nt Ct 50 100 150 200 .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S6. Single residue aligned heatmaps of LC isoforms with and without M83. Top panels: Percent deuterium uptake (%D) for all nine LC isoforms in the absence of M83. Middle panels: Percent deuterium uptake (%D) for LC isoforms in the presence of M83. Levels of deuterium uptake is color- coded as per legend, with red indicating high uptake (low protection) and blue indicating low uptake (high protection). Bottom Panels: Percent deuterium difference (Δ%D) plots showing the effect of M83 on deuterium uptake for each LC isoform. Blue regions indicate areas of increased protection upon M83 binding, while green regions represent areas with reduced protection. The solid horizontal line indicates the boundary between VL and CL domains. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint AL GL MM H3 H6 H7 H9 H16 MGC -0.6527 -2.2877 -5.656 -9.7348 -12.726 -8.5525 -1.2689 -1.5382 -2.1978 -5.9423 -10.118 -9.3657 -5.3146 -6.0593 -6.2951 -9.8071 -8.3952 -5.5635 -6.9897 -3.8743 1.27941 0.71019 0.45979 1.82762 -4.2073 -8.8321 -6.6803 -8.8155 -15.729 -19.909 -3.8015 -7.8453 -8.0349 -9.6825 -15.871 -18.695 -5.1393 -9.1071 -7.6768 -8.734 -15.478 -18.021 -6.439 -12.371 -11.018 -9.987 -11.062 -12.393 -5.9752 -10.522 -10.544 -9.4477 -9.2883 -10.224 -4.1576 -8.7871 -10.854 -9.2273 -6.8521 -7.1593 -2.8886 -8.9555 -3.0179 -0.9784 -0.5657 -1.5857 -1.9075 -4.1409 1.18826 1.13811 3.50257 3.41468 -0.7894 -5.0318 -1.7114 -1.2475 -1.2518 -1.891 -2.3719 -5.1918 -0.1041 -0.7691 1.06753 0.61679 -3.3643 -5.5252 -1.9717 -2.8779 -2.8757 -1.7616 -1.8344 -5.4696 -1.3792 -2.5231 -3.5896 -1.2664 -2.0566 -5.1061 -1.0963 -3.4787 -3.3372 -1.3395 -0.5769 -4.1767 -1.2837 -2.6312 -4.8704 -3.3192 -1.4879 -4.8133 -1.5172 -3.7841 -5.766 -4.2865 -2.0672 -5.2251 -1.8868 -2.7732 -4.1936 -1.9887 -1.1903 -5.174 -1.4845 -4.1802 -6.5294 -4.9882 -1.5555 -3.4663 -1.3727 -4.4032 -7.3922 -7.1383 -1.1318 -3.5248 -1.3254 -4.558 -6.6654 -5.0823 -2.6109 -1.6682 -0.7131 -4.7186 -7.8564 -8.6813 -2.3868 -0.0227 -1.8989 -7.2908 -14.198 -18.17 0.79338 -3.8835 -3.9933 -8.6963 -20.251 -21.586 0.55418 -1.5222 -0.5254 -3.3466 -14.096 -19.868 -1.2322 -1.1543 -1.7722 -6.7928 -15.515 -17.484 -0.3069 -0.8367 -1.1217 -7.014 -16.645 -18.568 -0.738 -0.7302 -2.6227 -9.1999 -17.141 -20.643 -0.529 -0.1945 -1.845 -6.9874 -15.096 -22.585 -1.0988 -0.8025 -1.1393 -7.1405 -15.861 -11.599 0.13445 -2.5523 -1.4665 -4.6395 -12.332 -28.312 -4.1707 -0.1344 -3.3418 -9.6443 -14.89 -17.208 -2.4275 -4.8685 -5.9628 -6.717 -14.696 -12.822 -3.8533 2.23595 -2.5018 -7.74 -12.592 -13.266 -4.1441 -7.2673 -12.025 -19.866 -25.754 -21.714 -2.8271 -8.5576 -13.721 -20.951 -26.853 -21.262 -3.0791 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65.48 68.114 70.954 76.029 65.581 72.236 75.742 79.642 84.258 94.204 33.308 43.506 49.176 54.321 53.998 67.432 8.1735 14.189 16.478 19.398 24.194 31.735 80.919 83.044 93.77 99.046 98.945 97.673 38.004 44.235 55.846 72.731 83.817 89.427 60.883 66.887 75.816 87.823 91.564 92.618 41.389 49.12 60.189 77.299 85.453 88.79 40.705 45.999 57.554 73.407 81.811 85.625 39.296 46.742 58.846 74.286 81.942 85.771 43.555 48.935 61.867 77.649 82.033 84.744 41.364 49.663 62.639 77.39 82.918 84.941 40.1 50.809 65.025 78.797 83.822 85.598 42.146 56.04 68.916 81.036 85.557 87.371 37.162 50.678 67.285 81.137 84.281 85.691 27.491 49.679 72.612 86.532 86.751 86.722 27.248 46.615 69.254 84.192 83.966 84.026 24.105 40.145 65.277 81.936 81.559 81.921 19.155 29.848 58.753 77.72 78.395 78.442 20.79 28.335 38.045 50.064 56.065 64.82 21.127 30.718 41.947 55.57 65.269 77.002 32.659 42.265 51.502 61.96 68.53 78.843 29.698 39.039 46.033 56.673 62.557 70.771 33.678 49.177 62.141 73.765 79.367 89.199 44.559 56.506 73.916 86.03 87.871 87.749 42.337 55.802 74.992 87.504 89.975 90.444 61.483 73.978 90.78 100.36 100.92 101.25 32.813 42.974 55.808 67.38 74.064 78.283 30.968 40.762 52.926 64.41 70.247 74.441 36.278 45.56 56.775 68.511 76.067 80.901 23.811 32.709 43.509 55.934 65.813 72.735 20.265 26.184 31.045 39.426 50.253 58.98 28.186 38.821 71.584 84.31 90.385 102.09 17.919 26.693 52.836 71.039 77.49 83.18 16.375 24.599 49.125 66.312 71.885 77.169 25.615 31.809 51.157 63.436 69.047 73.365 27.6 34.255 50.901 62.087 66.155 71.864 32.971 37.241 46.304 51.682 54.32 59.94 59.768 64.336 73.933 79.864 79.343 84.172 50.995 62.633 71.608 75.527 78.355 85.31 62.082 70.515 78.626 82.873 88.316 94.848 37.702 56.789 69.908 77.977 85.559 91.764 39.002 56.148 70.543 80.102 90.087 95.206 40.174 57.957 64.826 73.478 82.884 90.29 40.704 56.837 69.014 77.798 85.25 90.948 66.496 79.976 85.067 90.313 94.635 96.207 47.328 60.883 68.063 75 77.535 79.022 52.906 66.516 73.38 77.705 80.578 82.047 40.742 54.159 60.616 64.199 67.309 69.376 16.97 28.102 34.096 37.023 41.476 44.076 17.317 29.534 33.086 36.763 41.486 43.35 27.836 45.103 56.014 60.767 67.177 72.272 28.216 45.569 57.172 63.175 68.791 73.802 31.172 39.648 61.356 73.583 80.67 84.592 32.602 40.904 61.319 75.256 81.023 85.234 34.656 43.439 66.805 77.85 82.372 84.295 36.782 46.531 69.121 78.038 81.005 83.234 42.897 52.961 74.336 82.841 85.691 88.526 37.801 47.354 67.633 76.283 79.468 81.622 36.979 45.796 64.702 72.565 75.549 77.822 24.771 33.033 46.319 58.552 66.753 80.254 33.933 40.392 52.076 61.33 68.798 81.652 28.559 34.052 42.642 51.916 60.9 76.078 28.467 32.796 41.385 48.837 56.561 70.005 37.219 37.766 40.465 45.492 53.608 72.208 30.01 31.726 32.278 35.812 43.33 58.243 40.232 63.441 73.734 75.796 76.773 79.052 38.383 59.883 70.096 73.639 77.426 80.931 45.789 70.67 82.328 84.684 85.229 87.814 43.168 65.55 75.924 82.179 85.354 90.166 8.099 13.068 20.053 22.423 29.178 43.66 7.5665 14.555 19.511 21.51 27.54 42.491 4.9544 9.3111 16.436 23.325 38.031 54.781 4.8213 9.5964 19.886 34.35 47.643 62.369 28.953 36.039 45.811 56.962 65.224 75.025 27.583 33.892 45.758 58.903 65.937 74.179 29.817 35.95 47.395 60.326 67.167 74.917 29.368 37.235 48.796 61.028 67.771 75.23 30.674 36.454 47.888 61.162 68.099 75.849 29.304 38.646 51.722 63.533 69.955 76.827 30.126 37.582 49.629 62.505 69.249 76.588 39.872 49.065 62.849 80.901 86.077 89.453 30.364 39.472 52.352 64.573 70.984 77.61 38.418 45.153 61.223 77.707 81.69 83.059 40.691 48.201 63.121 78.641 82.067 85.08 28.977 41.372 56.053 68.393 73.378 78.653 40.14 49.302 63.947 78.461 81.923 85.777 38.478 49.993 66.225 80.276 83.754 86.447 51.668 67.964 86.63 100.35 99.693 100.57 28.332 50.78 74.551 86.834 88.055 88.099 26.93 47.082 70.608 84.407 84.848 85.456 24.007 40.831 66.353 81.737 82.373 83.055 18.905 30.077 59.744 78.065 78.917 79.375 22.452 31.312 41.552 51.216 57.413 65.96 23.754 34.764 46.248 56.436 65.675 77.78 37.238 47.315 56.253 63.754 72.13 83.611 23.463 35.466 48.572 58.478 66.124 81.634 32.326 40.595 49.308 56.734 64.35 72.396 38.978 56.613 69.007 75.784 81.319 90.66 43.011 57.542 74.537 84.08 88.097 90.308 41.051 56.58 74.808 86.337 90.055 91.106 44.377 57.745 74.421 87.76 89.585 90.297 53.148 69.214 84.967 97.15 100.08 100.58 54.816 71.835 87.003 96.189 96.884 98.361 32.127 43.088 54.984 66.508 74.844 77.499 30.853 41.132 52.525 63.577 70.618 74.064 24.848 32.994 42.216 55.954 65.19 72.495 19.405 25.847 30.294 38.81 49.573 57.518 25.552 36.944 67.843 78.862 84.815 96.596 18.107 28.309 52.287 67.888 72.866 78.685 18.705 27.944 53.421 70.586 77.025 83.115 17.204 25.681 49.938 65.895 72.004 77.952 18.826 27.504 50.326 69.921 75.69 81.341 25.336 33.303 51.373 62.354 67.486 73.318 14.461 21.762 33.208 43.994 48.351 52.402 26.895 34.666 50.175 60.548 65.107 72.127 32.09 39.673 44.796 50 53.247 58.895 34.906 44.93 58.084 66.159 69.73 76.478 51.541 60.624 65.814 70.517 71.256 78.122 59.464 69.24 75.731 81.919 82.564 85.245 38.095 56.482 64.864 67.648 72.578 83.614 49.047 63.665 72.246 74.955 78.223 85.896 60.329 71.405 79.448 82.979 87.113 94.613 24.034 33.189 43.043 48.922 58.777 73.978 22.492 33.958 49.38 60.626 67.42 74.573 39.506 50.294 66.243 77.195 81.087 86.303 37.502 46.23 62.374 73.634 78.42 82.141 34.17 44.351 60.669 72.19 77.029 82.218 23.146 31.647 52.248 68.267 71.722 72.633 16.384 23.074 39.613 51.482 54.939 55.899 14.732 20.585 35.318 47.01 50.547 54.653 14.42 20.145 35.204 51.726 57.977 61.983 22.119 29.532 45.434 61.456 70.214 76.072 30.752 37.069 51.113 65.752 72.429 78.166 29.179 34.514 48.709 63.971 71.27 76.542 27.032 32.608 46.092 61.582 68.175 72.749 38.558 43.962 55.413 69.453 76.038 82.884 39.967 46.105 56.264 67.623 74.212 81.251 50.025 51.697 55.96 67.47 68.421 75.455 33.988 35.695 46.486 61.186 70.123 87.19 25.443 29.261 38.98 46.269 53.332 68.136 26.626 32.027 42.829 50.018 57.84 75.271 25.751 30.383 40.573 45.171 53.182 67.319 31.766 36.796 49.326 57.829 64.207 79.364 30.221 34.298 46.383 51.98 60.573 77.247 27.182 36.783 49.891 60.941 66.895 72.382 7.9535 13.245 26.953 40.006 47.96 56.567 31.54 38.814 51.285 64.068 72.599 78.404 24.459 29.413 41.755 55.81 65.35 72.81 33.436 40.23 52.358 65.623 72.066 77.428 27.711 33.314 45.787 59.729 67.262 73.052 27.727 35.299 48.368 61.537 69.067 74.377 41.821 47.985 60.256 76.297 84.95 88.664 32.426 39.749 52.03 63.043 70.908 75.809 51.297 62.14 81.077 95.027 94.685 97.749 28.205 49.281 72.895 86.653 86.976 86.536 28.391 46.924 69.117 84.308 84.323 84.566 25.004 40.788 65.303 82.186 82.476 82.705 25.132 41.664 67.811 83.426 84.023 84.176 23.221 30.977 41.227 51.886 57.839 64.398 23.154 33.553 45.212 56.78 65.26 74.196 30.458 40.573 48.179 57.469 63.198 70.74 36.762 50.622 62.552 70.925 76.443 85.136 44.468 56.063 70.891 83.822 87.934 87.251 42.895 56.572 72.114 86.543 90.198 90.903 51.582 65.832 77.964 94.395 98.219 98.802 56.196 66.708 81.392 93.636 94.956 95.591 32.584 42.442 53.969 66.85 73.879 78.168 31.127 40.605 51.804 64.306 70.699 75.236 35.495 44.644 55.698 68.536 76.599 80.512 20.668 25.4 31.967 40.829 49.929 58.158 26.414 36.56 66.206 78.263 84.416 96.551 18.123 26.95 52.981 72.816 78.977 84.741 16.05 25.083 49.315 67.271 73.732 78.971 17.081 25.579 51.327 68.257 73.446 77.377 26.653 33.394 51.694 65.891 70.123 74.464 27.177 36.421 55.851 69.699 70.974 72.879 28.143 34.938 51.739 62.279 67.879 72.356 35.906 43.94 57.817 68.982 72.079 78.222 61.944 66.415 74.52 82.544 81.727 84.871 50.696 61.691 71.219 76.482 79.704 87.689 48.872 60.209 67.777 77.711 83.283 91.139 43.773 57.501 70.96 80.427 85.494 91.466 40.826 55.47 68.333 76.624 82.393 89.729 39.544 48.249 66.24 80.228 84.491 92.916 24.899 30.418 43.903 57.087 62.472 70.076 24.509 29.419 41.701 52.241 60.885 72.725 27.691 32.697 45.301 58.396 64.261 70.809 28.847 33.64 47.046 58.574 64.141 70.221 28.089 36.94 47.846 57.601 65.994 70.265 30.773 37.222 49.448 60.531 65.05 73.048 50.221 61.586 80.882 91.22 94.194 98.407 40.638 50.102 67.768 80.943 84.728 92.095 32.608 42.137 55.222 66.39 70.689 80.373 35.905 43.739 57.475 66.268 72.528 82.501 33.839 41.241 53.903 63.531 67.881 78.452 5.0859 10.809 20.704 25.845 27.176 32.774 7.8648 13.602 18.634 20.115 25.277 41.725 21.286 26.528 32.42 36.411 40.893 56.684 32.136 39.959 47.861 53.935 60.728 82.042 26.081 31.029 38.37 43.022 49.109 65.902 27.097 33.905 41.761 46.738 53.179 71.355 27.286 32.589 40.141 45.008 49.941 65.447 43.545 41.53 57.631 60.56 63.097 78.19 28.629 34.034 42.82 50.274 54.465 70.418 9.7538 15.11 28.957 36.121 42.581 58.938 29.498 34.593 47.359 57.881 66.29 77.942 27.146 32.851 43.6 54.56 63.945 73.893 25.989 31.294 43.542 55.761 64.808 74.438 33.02 41.268 54.207 63.977 70.855 78.453 32.942 41.876 55.29 65.089 71.203 78.336 32.805 42.794 57.053 66.486 72.315 79.201 30.857 40.081 53.792 64.265 70.307 78.943 27.401 32.085 45.029 57.131 64.731 73.272 29.209 33.845 46.658 58.376 65.842 74.772 29.448 35.247 48.182 59.617 66.593 76.762 29.312 36.86 51.277 62.419 68.957 76.923 32.769 35.983 50.703 63.242 70.531 76.786 47.32 54.407 68.417 77.505 85.401 93.53 48.569 61.671 76.261 83.64 87.989 92.691 27.125 49.563 74.505 86.307 86.423 86.874 28.693 47.229 72.021 84.5 84.227 85.456 25.03 41.459 67.857 82.264 81.869 82.264 19.677 30.489 61.422 78.882 78.218 79.642 23.622 30.968 42.497 50.658 58.271 66.4 25.515 35.254 47.766 58.836 67.335 80.777 27.602 35.975 50.242 58.709 69.396 82.693 33.301 41.036 50.201 58.209 65.075 72.584 37.726 53.468 62.935 72.161 80.065 95.774 44.579 56.034 75.234 84.266 89.235 91.704 43.078 56.642 76.271 87.699 89.554 91.441 35.578 45.815 61.57 73.632 77.672 84.405 34.155 43.852 57.603 69.661 76.938 82.536 32.748 42.07 55.443 67.61 73.433 79.538 38.4 46.208 58.899 72.421 80.036 84.177 24.312 31.055 37.217 50.352 61.07 70.917 21.222 26.606 32.588 44.962 54.912 64.877 26.096 36.772 68.113 79.179 85.75 97.44 20.743 29.152 56.333 73.482 77.495 86.41 18.565 26.931 52.332 68.476 72.891 79.939 21.733 29.835 57.294 71.749 76.667 83.993 21.731 30.559 55.909 72.343 76.311 78.706 27.643 34.691 52.913 64.636 69.417 76.749 28.99 36.468 51.822 62.7 66.117 74.636 37.331 46.989 59.411 68.082 72.113 80.01 51.866 62.464 67.98 74.091 76.262 84.77 51.934 63.009 71.835 74.902 79.434 88.158 51.16 63.664 72.025 75.264 79.572 87.798 62.232 71.515 79.982 84.654 87.164 99.365 33.175 44.747 58.663 69.693 73.742 80.692 38.31 50.009 64.518 75.83 79.501 84.771 44.797 59.782 78.604 91.789 92.942 94.726 45.983 62.55 80.378 92.015 93.161 94.937 59.204 78.52 96.441 100.47 100.96 101.35 58.041 81.817 96.923 101.51 100.48 100.07 50.791 76.311 92.12 100.2 97.709 98.665 24.447 28.981 39.84 45.494 45.452 46.711 22.697 28.735 39.371 44.951 47.317 48.823 19.975 25.792 35.076 41.07 43.037 44.402 24.076 30.711 42.004 49.357 51.131 52.431 21.232 27.027 37.568 44.138 45.498 47.116 33.591 43.123 60.57 70.23 73.021 73.851 28.287 36.816 51.465 60.499 62.448 64.295 25.311 32.293 45.614 53.701 55.394 58.108 35.326 42.512 56.82 76.153 87.218 98.235 38.968 46.29 63.866 83.03 93.841 101.15 29.15 35.589 50.735 68.897 79.369 89.372 34.218 40.367 58.717 78.774 84.732 92.224 45.891 53.388 69.103 84.677 91.452 97.067 31.974 37.884 56.588 73.682 82.794 89.756 32.16 37.565 52.718 70.709 81.756 90.046 34.599 40.458 56.053 75.073 84.388 91.61 36.06 41.518 52.2 66.864 74.747 85.072 38.376 43.885 55.659 70.077 77.743 86.432 32.206 37.737 47.25 59.949 69.056 78.058 38.902 44.439 54.686 67.542 72.49 81.48 42.453 48.743 57.908 69.722 75.847 84.47 39.715 43.896 54.347 65.601 71.054 77.931 41.736 43.455 47.041 55.934 60.033 71.438 38.627 43.367 49.104 51.894 55.35 66.429 16.288 19.787 24.368 27.39 30.746 40.814 4.3335 7.9638 17.951 22.5 26.704 39.188 27.949 30.979 39.728 42.878 48.567 58.779 27.117 30.537 38.748 42.216 47.411 57.993 31.85 36.317 46.475 49.635 54.272 68.048 22.262 24.681 31.857 34.309 39.081 49.591 20.955 23.223 29.409 31.449 36.081 46.397 25.208 28.064 35.405 39.837 44.2 55.523 23.851 26.166 32.522 36.004 39.976 50.879 29.136 31.734 38.819 41.122 43.184 51.048 37.753 42.238 55.404 65.493 67.116 68.999 44.623 49.151 61.282 73.902 75.34 77.773 44.063 57.616 70.63 77.631 82.579 89.91 23.687 34.911 43.459 50.444 58.358 70.511 12.817 18.203 25.459 32.494 43.251 55.196 11.361 15.82 23.797 31.332 40.78 54.511 54.394 61.25 71.703 84.398 92.467 99.125 47.938 54.952 63.973 74.285 81.804 87.837 42.499 48.767 62.051 76.292 83.42 89.055 43.077 48.733 62.061 74.827 80.743 84.139 42.06 49.669 63.826 76.188 81.486 85.121 40.703 50.989 65.884 77.152 82.017 85.247 42.271 55.72 69.778 80 84.363 87.452 37.483 50.311 67.64 79.819 82.685 85.577 55.467 67.426 88.629 103.5 99.894 102.07 28.791 50.583 74.812 87.435 87.303 87.819 29.214 47.001 70.081 83.968 83.548 84.538 25.699 41.471 66.408 81.328 81.537 82.538 20.612 31.081 60.152 77.718 77.687 78.212 31.772 32.509 42.335 52.211 58.287 65.149 34.824 36.297 46.875 57.328 65.984 75.629 43.062 47.137 54.199 60.997 68.916 76.588 38.853 41.121 49.521 56.515 62.6 69.179 54.696 55.7 68.482 75.917 79.487 87.399 43.544 55.872 72.019 82.31 85.65 85.905 43.335 57.085 74.491 86.312 89.703 89.516 52.862 65.148 82.053 94.339 98.414 99.829 56.412 70.029 84.302 92.687 94.755 91.3 34.3 43.552 55.228 67.574 73.583 77.837 31.465 41.043 52.151 64.848 69.915 73.617 36.186 45.077 56.316 69.131 76.416 80.551 24.799 32.465 42.195 56.181 65.457 70.856 20.805 26.172 31.492 41.531 50.387 57.601 27.803 38.466 65.582 79.529 84.998 96.67 16.114 24.273 49.65 65.672 70.7 77.514 14.267 27.083 52.25 71.2 76.917 83.583 17.189 24.141 50.033 66.105 71.641 76.759 18.458 27.714 54.907 71.693 75.863 76.33 18.507 23.387 36.547 45.667 49.027 52.4 13.351 20.671 34.89 45.73 49.061 52.37 30.341 36.815 47.216 52.287 55.934 59.193 33.793 38.51 45.815 52.286 54.665 59.82 54.153 60.365 65.926 71.271 69.411 77.916 61.108 67.723 76.39 81.769 81.71 87.647 36.124 51.563 62.392 67.179 71.312 81.222 39.646 54.963 67.77 71.335 77.539 89.817 51.424 64.057 72.334 77.301 81.477 92.095 63.089 70.649 79.262 83.546 87.711 95.449 6.1844 8.8073 21.963 35.74 52.319 63.791 50.127 60.656 76.159 84.129 88.129 92.694 54.456 64.686 78.956 86.216 89.645 93.587 43.815 49.138 62.065 68.283 68.908 70.091 45.649 48.428 58.421 69.142 72.103 68.793 25.792 40.799 71.592 80.572 85.024 94.875 35.042 44.587 56.981 60.949 61.876 61.917 23.971 34.578 48.2 53.429 53.945 54.557 26.76 36.448 45.986 51.338 51.818 53.177 20.835 31.402 44.384 51.168 51.95 51.82 36.676 53.033 68.07 72.569 72.946 73.73 29.643 42.233 56.855 66.528 66.625 67.703 30.353 46.213 62.864 72.61 74.889 73.361 7.3518 12.005 20.782 29.723 45.322 66.053 26.756 37.006 49.503 62.421 70.365 75.113 57.906 72.673 84.976 93.908 96.646 99.367 52.48 65.998 80.743 89.949 94.493 98.375 61.445 71.269 84.4 92.743 95.804 99.325 47.866 60.443 74.934 84.472 88.618 92.482 49.151 59.321 73.871 83.565 88.523 93.48 49.405 54.627 68.392 74.834 80.658 87.826 28.176 34.392 38.617 45.912 58.556 71.201 36.719 43.379 49.581 60.038 73.991 87.565 35.122 40.935 46.301 56.473 69.518 83.273 34.371 39.626 45.204 54.252 66.173 79.966 24.645 28.543 32.821 38.916 48.811 60.175 22.546 26.301 29.196 36.229 45.378 54.511 28.479 31.958 37.227 44.424 54.962 67.667 25.332 28.98 33.17 39.682 49.057 60.283 22.719 26.465 30.767 37.6 45.82 56.33 26.066 32.579 33.874 39.155 45.128 55.715 30.417 63.995 84.926 96.888 100.74 98.712 30.763 55.289 89.713 100.74 101.57 100.5 30.78 61.869 96.324 99.466 101.38 100.04 17.332 28.472 47.592 58.895 72.858 80.91 13.16 25.164 44.242 55.408 63.517 74.836 10.035 21.316 41.239 52.241 61.192 74.289 5.5417 9.0072 20.184 33.703 46.222 62.879 5.7348 9.8021 18.357 31.354 45.785 61.618 6.8013 10.909 20.084 29.815 44.545 65.657 6.5983 12.124 19.283 30.333 45.131 66.416 6.3364 10.606 18.964 28.901 44.021 64.473 53.701 61.859 69.807 87.104 95.08 99.874 48.066 56.497 64.149 77.002 85.093 88.933 41.054 49.05 59.06 76.996 84.807 89.219 40.062 46.472 58.241 74.499 80.488 83.995 42.872 48.988 60.613 76.113 81.608 85.324 41.492 50.015 62.408 77.164 82.245 85.037 40.296 51.201 64.796 78.665 83.297 86.434 56.394 66.982 74.595 85.042 91.879 96.052 42.476 56.996 68.726 81.413 85.952 88.354 54.712 67.241 76.538 85.806 92.568 98.035 36.766 50.25 66.473 80.227 84.046 86.044 24.848 41.221 64.277 81.273 81.744 82.336 28.915 51.487 73.768 87.577 86.716 88.204 25.129 41.684 66.51 82.352 81.866 82.17 19.247 30.081 58.754 78.017 77.954 78.902 22.596 30.237 39.74 49.506 54.974 64.213 23.91 33.81 44.67 56.127 63.638 77.231 34.691 45.342 52.938 65.91 70.952 79.432 31.735 39.945 49.663 58.483 63.775 72.691 38.925 55.652 66.874 76.25 80.611 90.379 44.373 56.083 73.397 84.437 87.178 88.975 41.987 55.706 74.604 87.365 89.829 90.174 57.054 73.165 87.071 96.539 98.82 100.06 55.404 67.868 84.044 97.181 94.841 95.306 33.551 45.531 58.496 70.665 77.503 81.399 32.89 42.557 55.181 67.332 74.176 78.95 30.767 40.475 51.972 64.159 70.582 74.908 25.128 32.298 42.793 55.648 64.932 73.969 23.631 30.407 35.699 45.916 57.219 65.953 20.129 25.757 30.281 40.385 50.772 58.811 26.987 37.156 48.644 60.207 66.064 79.002 25.261 35.78 66.593 78.409 83.249 95.16 16.862 27.108 51.797 68.943 73.533 78.353 18.03 28.232 52.806 71.011 78.171 83.817 16.502 24.314 49.14 66.575 70.838 77.79 12.636 20.218 52.1 66.126 67.582 83.397 18.489 27.5 54.712 71.513 75.426 77.221 25.411 32.38 50.929 63.349 66.137 73.284 12.024 17.629 33.725 47.042 48.527 53.605 27.078 34.183 50 61.034 65.45 71.561 31.473 36.826 46.22 52.26 56.676 60.008 36.943 47.573 60.697 69.462 74.051 77.864 53.479 61.15 67.228 72.3 69.627 75.778 57.667 68.905 75.882 81.785 81.501 83.732 50.766 61.335 68.63 72.031 75.67 81.402 49.28 63.468 70.487 74.233 76.623 83.59 40.087 58.709 68.267 67.991 78.419 84.627 50.473 63.941 72.328 75.951 79.333 86.908 61.088 72.803 79.843 83.763 86.401 96.095 32.603 43.529 56.247 65.685 70.021 75.108 34.877 46.37 59.633 69.257 73.64 78.154 29.806 40.757 54.752 65.011 70.578 73.285 34.308 49.269 67.953 76.496 81.858 84.85 41.885 58.798 77.341 85.929 90.449 92.778 45.159 64.194 80.368 89.28 93.54 95.929 55.742 81.145 98.355 101.61 100 100.99 25.435 30.303 43.182 46.928 48.246 48.709 22.984 27.338 38.816 42.483 44.359 44.569 21.113 24.609 35.601 38.553 40.675 42.13 25.246 29.899 42.276 45.892 47.475 47.817 39.974 47.044 67.125 72.935 75.297 75.051 33.647 40.286 57.442 62.607 65.08 65.572 29.839 35.478 50.398 55.562 57.627 60.335 25.494 30.691 45.344 50.123 54.353 59.564 23.845 29.979 45.704 50.84 56.808 62.582 36.218 41.282 56.962 72.975 83.623 95.063 40.405 46.371 62.962 80.092 89.359 98.611 32.049 39.176 56.391 70.818 80.138 89.458 45.58 49.574 67.387 84.037 92.551 100.51 19.275 28.325 54.036 70.644 74.947 77.365 48.875 55.531 71.045 85.531 91.592 100.84 33.842 39 55.761 70.432 81.745 89.876 42.326 48.324 70.858 82.326 88.629 93.408 36.426 42.051 59.237 75.461 83.744 91.391 39.613 46.24 62.634 78.252 84.647 90.762 42.715 48.565 66.989 79.532 84.93 92.059 37.785 42.518 54.008 66.932 74.247 83.968 35.085 39.385 50.995 62.606 69.724 78.978 40.084 44.557 57.429 69.767 76.728 85.126 43.498 48 60.049 70.834 75.709 83.822 39.647 44.203 56.186 67.018 71.85 79.196 44.559 49.091 61.289 71.229 76.309 84.117 40.653 45.429 56.629 66.478 71.332 78.322 40.134 42.942 52.233 61.927 66.378 72.89 42.513 44.507 48.662 56.922 60.944 68.473 24.175 25.315 27.56 30.668 36.367 48.334 3.4435 6.3177 17.287 18.87 22.036 36.115 28.117 31.295 40.148 42.116 45.627 54.162 18.085 18.789 25.682 27.66 29.997 36.095 27.241 29.51 38.68 41.122 43.028 52.529 32.874 36.362 47.193 50.332 54.817 64.884 31.799 35.807 46.185 49.58 51.103 64.228 35.652 40.445 51.663 52.298 57.242 59.283 21.97 24.57 31.175 34.04 37.202 45.215 20.794 22.851 28.811 31.725 35.068 42.015 28.156 30.748 38.372 39.834 44.302 52.658 22.211 25.312 31.514 34.529 38.427 45.34 27.921 30.48 38.899 40.116 42.34 47.6 25.226 28.601 34.532 37.072 39.151 43.259 40.126 43.556 52.725 65.546 65.784 66.004 29.459 36.255 40.191 46.848 52.352 60.44 9.9641 12.549 18.707 25.242 29.533 40.934 9.6255 12.776 19.461 26.076 32.079 43.542 9.9316 13.113 20.344 26.04 32.439 43.592 9.2472 11.378 17.721 24.063 29.529 41.801 53.757 61.752 73.185 82.553 91.467 98.925 49.007 56.332 65.122 74.348 82.772 89.322 42.696 49.893 62.545 74.996 83.893 89.305 43.41 49.355 62.665 74.583 80.629 84.747 42.143 50.467 64.327 75.798 81.392 85.458 40.797 51.427 66.575 77.306 82.419 86.256 28.435 50.271 75.011 86.714 87.095 87.403 28.606 47.703 71.333 84.705 84.827 84.613 24.808 41.265 66.902 82.499 82.898 82.653 19.845 30.504 59.867 77.875 78.445 78.223 34.552 36.17 45.709 56.773 65.595 77.045 40.185 40.981 49.399 56.792 63.617 70.929 54.643 55.777 66.488 72.987 78.318 88.592 45.33 55.933 73.229 83.366 87.397 87.848 52.72 65.183 81.079 96.285 99.263 98.511 56.79 70.293 84.642 95.962 96.151 96.277 33.041 43.124 55.48 68.444 75.067 78.423 31.245 40.738 52.745 64.975 71.135 74.364 35.959 45.065 57.346 69.193 76.367 80.994 25.237 33.16 42.774 57.73 67.329 72.878 23.807 30.136 35.71 47.582 58.593 65.368 20.21 25.932 31.144 42.174 52.455 59.324 25.838 36.136 68.21 79.452 84.79 95.701 18.124 27.734 51.069 67.444 72.549 79.332 18.167 26.263 52.082 69.431 76.21 82.598 16.445 24.147 48.312 64.501 69.538 76.967 34.924 42.009 61.356 77.257 85.749 93.238 26.115 33.116 51.016 62.876 67.356 73.631 27.907 34.338 49.718 61.328 64.676 71.987 60.069 68.94 77.02 81.933 81.811 87.475 34.4 52.74 62.579 65.835 73.142 85.657 50.862 61.718 68.911 72.639 77.632 87.157 52.186 63.978 71.451 76.607 81.066 91.169 41.036 57.277 66.323 70.428 79.46 92.685 52.789 65.801 73.42 77.422 83.48 93.649 65.014 73.726 80.638 84.788 88.862 95.621 31.743 43.661 56.181 66.941 74.754 83.074 33.425 46.396 59.334 69.416 75.568 81.672 54.44 69.601 77.986 86.077 90.316 92.992 68.152 90.172 97.231 99.609 99.849 101.05 28.735 32.329 44.381 51.182 55.107 60.124 26.362 29.499 41.369 50.808 57.735 62.339 31.371 36.46 48.017 55.556 58.628 63.175 44.493 51.062 67.207 75.762 77.859 79.969 37.53 43.592 59.898 73.35 79.596 82.394 30.776 39.221 61.056 78.267 85.764 87.675 43.622 60.761 82.927 94.43 95.369 95.633 52.277 73.503 93.678 100.44 103.35 102.33 43.506 64.049 88.055 95.577 98.227 97.101 55.678 73.146 90.598 99.516 101.47 100.97 47.375 64.34 84.845 93.237 95.929 97.973 45.048 61.058 80.017 90.703 95.663 98.82 45.564 58.558 77.32 88.058 94.182 98.355 43.503 55.543 71.694 82.023 87.204 91.283 45.294 56.336 70.975 80.891 86.471 90.773 53.238 63.293 76.76 86.882 92.159 96.154 45.819 54.699 68.93 79.548 85.836 90.1 43.134 52.469 65.267 75.406 81.477 85.759 45.986 55.281 68.646 78.955 85.194 89.644 45.388 49.01 55.085 66.39 76.104 82.044 29.327 34.468 38.163 48.756 60.209 67.197 6.3957 9.9233 23.988 29.785 38.727 52.393 19.682 22.565 32.293 36.736 43.702 56.512 26.674 31.016 40.489 45.15 51.693 60.893 26.324 30.575 39.237 43.713 50.894 61.584 21.424 24.546 32.177 37.727 44.681 54.41 21.353 24.04 30.567 34.55 40.714 49.486 25.664 28.958 37.966 41.143 47.378 59.176 23.456 21.439 23.701 25.943 28.857 32.994 43.387 55.224 62.508 65.272 67.971 72.444 48.852 58.517 66.592 71.568 72.162 75.967 51.121 64.175 72.796 76.395 78.063 82.545 30.033 37.733 46.982 53.452 58.634 67.115 31.355 36.195 44.396 52.12 58.317 68.26 9.0469 11.859 22.188 32.516 40.859 55.672 10.291 14.776 25.402 35.944 43.993 59.137 9.8471 14.161 21.584 27.737 34.319 49.974 10.005 12.955 23.513 34.087 42.232 55.22 53.129 65.447 74.629 82.893 92.019 98.658 47.454 57.739 66.563 74.55 83.473 88.637 41.644 51.603 63.827 75.481 84.115 89.543 40 48.454 61.992 72.493 79.68 84.359 42.032 50.749 63.689 74.251 80.72 85.389 41.202 51.771 65.677 75.584 81.934 86.036 39.831 52.642 67.581 76.849 82.691 86.632 41.269 57.165 71.328 79.836 84.853 88.013 36.29 50.819 68.626 79.526 83.48 86.188 26.951 50.161 73.724 85.842 86.356 86.708 27.435 47.096 69.989 83.463 84.499 84.789 25.767 42.499 67.309 82.372 83.738 83.632 20.875 31.98 59.855 78.559 79.314 78.874 30.331 33.262 42.663 53.456 60.711 67.688 33.77 37.064 47.565 58.633 67.54 78.307 37.41 41.639 48.873 56.319 63.341 70.46 51.709 56.205 68.328 74.339 79.896 90.15 43.91 56.165 73.218 84.015 87.564 89.158 39.912 55.04 73.34 84.341 89.17 89.764 40.595 56.773 73.718 84.333 89.851 90.332 50.224 62.367 80.201 94.215 97.711 98.036 52.068 70.886 84.263 93.106 95.74 98.845 30.575 40.95 53.215 65.049 72.298 75.052 25.874 33.648 43.723 58.593 68.004 73.742 24.493 30.685 36.939 48.218 59.219 66.457 21.647 27.031 32.604 42.9 53.133 59.666 21.606 29.861 59.693 79.109 88.765 98.137 16.871 24.273 48.346 64.961 72.071 77.755 19.312 28.174 53.691 70.239 75.499 77.354 18.659 22.784 36.239 50.381 56.027 63.246 14.871 19.595 31.429 41.769 47.746 53.001 31.664 38.41 45.421 50.777 54.293 61.999 47.696 58.377 64.305 67.829 70.432 76.071 57.899 69.91 77.708 82.777 84.161 88.335 34.943 52.831 63.086 67.137 73.829 85.911 48.887 62.205 68.652 72.153 77.536 86.78 40.003 58.802 66.682 70.296 78.66 93.845 50.258 66.003 73.147 76.97 83.331 93.859 60.563 74.081 79.192 82.292 86.98 95.584 AL GL MM H3 H6 H7 H9 H16 MGC AL GL MM H3 H6 H7 H9 H16 MGC 10 sec 1 min 10 min 1 hr 4 hrs 16 hrs Time in D2O 10 sec 1 min 10 min 1 hr 4 hrs 16 hrs Time in D2O 10 sec 1 min 10 min 1 hr 4 hrs 16 hrs Time in D2O 15 30 45 60 75 90 100 Percent Deuterium Uptake No data 0 -25 -15 -10 -5 0 5 10 % Deuterium Difference 15 20 25 30 No data -30 -20 No change 15 30 45 60 75 90 100 Percent Deuterium Uptake No data 0 VL CL VL CL VL CL VL CL VL CL VL CL Deuterium Uptake of LC Isoforms – Percent Deuterium Uptake Effect of M83 on LC isoforms – Percent Deuterium Difference Deuterium Uptake of LC Isoforms + M83 – Percent Deuterium Uptake .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S7. Peptide chiclet plots showing deuterium uptake of various LCs and the effect of M83. Top panel: Percent deuterium uptake (%D) for all nine LC isoforms in the absence of M83. Levels of deuterium uptake are color-coded as per the legend, with red indicating high uptake (low protection) and blue indicating low uptake (high protection). Middle panel: Percent deuterium uptake (%D) for all nine LC isoforms in the presence of M83. Bottom panel: Percent deuterium difference (Δ%D) plots showing the effect of M83 on deuterium uptake for each LC isoform. Blue regions indicate areas of increased protection upon M83 binding, while green regions represent areas with reduced protection. The solid horizontal line indicates the boundary between the variable domain (V L) and the constant domain (CL). .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint Figure S8. Limited proteolysis assay of FL LCs with and without M83 monitored by SDS-PAGE. FL LCs were tested at a concentration of 8.3 μM, with M83 at 50 μM (1:6 molar ratio) in 10 mM phosphate buffer, pH 7.4, 150 mM NaCl, at 37°C and 450 rpm. Proteolysis reaction was initiated by addition of trypsin at 0.232 μM. Time points (0, 1, 30, 180 minutes, and 24 hours) are shown for digestion experiments. "+" and "-" refer to digestion in the presence and absence of M83, respectively. Gels (10- 20%) were run under reducing conditions and stained with Coomassie Blue. Alcohol dehydrogenase was included as a loading control (not shown). Data were fitted to a single exponential decay model and the area under the curve (AUC) was calculated. Dashed lines show data where the fits did not converge. For comparison, the average AUC for all residues was calculated for each FL LC. .CC-BY 4.0 International licenseavailable under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made The copyright holder for this preprintthis version posted January 8, 2026. ; https://doi.org/10.64898/2026.01.07.698275doi: bioRxiv preprint