Molecular Modeling and Docking of Aquaporin Inhibitors to Reveal New Insights into Schistosomiasis Treatment

Abstract

Background: Schistosomiasis (snail fever/bilharzia), a disease caused by parasitic flat-worms (schistosomes), infects millions of people worldwide. Aquaporins from these organisms were found to be a potent drug target. Introduction: We investigate the possible mechanism of inhibition of Aquaporin (AQP) from S.mansoni by 5 drug molecules (Praziquantel, Metrifonate, Artimisinin, Albendazole, and Amos-canate). Methods: 3D molecular structure of Aquaporin was obtained through homology modeling and further protein-ligand docking and MD simulation were performed. Results: VAL-75, ASN-91, ALA-220, ASN-222, ARG-225 amino acids were found to play cru-cial role in ligand binding. TRP-71 and other important residues play major role in hydrophobic interactions stabilizing protein-ligand complexes. Conclusion: We hope that this study (with the newly identified aquaporin target) will support the development of structure and pharmacophore-based novel S. mansoni drugs to control and curb Schistosomiasis. © 2020 Bentham Science Publishers.