Saponins as a Potential PFN2 Inhibitor: In silico Approach

Abstract Colorectal cancer (CRC) disease has a high mortality rate and has recently involved human profilin II (Pfn2), an actin-binding protein, as a promoter of its invasiveness and progression. This work evaluated the binding affinity of oleanolic acid saponin over Pfn2 and its structural stability. QM and MM techniques were applied to perform geometrical optimization and calculation of the reactive sites from oleanolic acid, whereas molecular docking and MD simulations for protein-ligand interaction under physiological conditions. Oleanolic acid saponin showed a high binding affinity to the Pfn2 PLPbinding site. Analysis of the protein-ligand structure suggests saponin as a molecule with high potential for developing new drugs against Pfn2 in colorectal cancer cells.