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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. We investigate the… Click to show full abstract
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. We investigate the possible mechanism of inhibition of Aquaporin (AQP) from S.mansoni by 5 drug molecules (Praziquantel, Metrifonate, Artemisinin, Albendazole, and Amoscanate). 3D molecular structure of Aquaporin was obtained through homology modeling and further protein-ligand docking and MD simulation were performed. VAL-75, ASN-91, ALA-220, ASN-222, ARG-225 amino acids were found to play a crucial role in ligand binding. TRP-71 and other residues have hydrophobic interactions stabilizing protein-ligand complexes. This study (with the newly identified Aquaporin targets) supports the development of structure and pharmacophore-based novel S.mansoni drugs to control and curb Schistosomiasis.
Journal Title: Current computer-aided drug design
Year Published: 2019
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