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

Author(s):

Meshari Alazmi*   Pages 1 - 14 ( 14 )

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.

Result: 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

Affiliation:

College of Computer Science and Engineering, University of Ha'il, P.O. Box 2440, Hail, 81481



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