Molecular Modeling and Docking of Aquaporin Inhibitors to Reveal New Insights into Schistosomiasis Treatment
| Autor: | Meshari Alazmi |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Drug
Molecular model media_common.quotation_subject Molecular Conformation Aquaporin Schistosomiasis Molecular Dynamics Simulation Biology Aquaporins Ligands 01 natural sciences chemistry.chemical_compound Drug Discovery medicine Animals Humans Homology modeling Metrifonate media_common 010405 organic chemistry Amoscanate Schistosoma mansoni General Medicine medicine.disease 0104 chemical sciences Molecular Docking Simulation 010404 medicinal & biomolecular chemistry chemistry Biochemistry Docking (molecular) Molecular Medicine Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Current Computer-Aided Drug Design. 16:772-785 |
| ISSN: | 1573-4099 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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