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

[ Vol. 16 , Issue. 6 ]


Meshari Alazmi*   Pages 772 - 785 ( 14 )


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.


Schistosomiasis, aquaporin, S. mansoni, molecular dynamics simulation, homology modeling, molecular docking.


College of Computer Science and Engineering, University of Ha’il, Hail 81481

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