Abstract
Background: Schistosomiasis (snail fever/bilharzia), a disease caused by parasitic flatworms (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 Amoscanate).
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 crucial 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.
Keywords: Schistosomiasis, aquaporin, S. mansoni, molecular dynamics simulation, homology modeling, molecular docking.
Graphical Abstract
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