Picot, Marie C. N.Zengin, GökhanMollica, AdrianoStefanucci, AzzurraCarradori, SimoneMahomoodally, Mohamad F.2020-03-262020-03-2620171573-40641875-6638https://dx.doi.org/10.2174/1573406413666170307163929https://hdl.handle.net/20.500.12395/35198Background: Mangiferin, was identified in the crude methanol extract, ethyl acetate, and n-butanol fractions of Aphloia theiformis (Vahl.) Benn. Objective: This study aimed to analyze the plausible binding modes of mangiferin to key enzymes linked to diabetes type 2 (DT2), obesity, hypertension, Alzheimer's disease, and urolithiasis using molecular docking. Method: Crystallographic structures of alpha-amylase, alpha-glucosidase, glycogen phosphorylase (GP), pancreatic lipase, cholesterol esterase (CEase), angiotensin-I-converting enzyme (ACE), acetyl cholinesterase (AChE), and urease available on the Protein Databank database were docked to mangiferin using Gold 6.0 software. Results: We showed that mangiferin bound to all enzymes by pi-pi and hydrogen bonds mostly. Mangiferin was docked to both allosteric and orthosteric sites of a-glucosidase by pi-pi interactions. However, several hydrogen bonds were observed at the orthosteric position, suggesting a preference for this site. The docking of mangiferin on AChE with the catalytic pocket occupied by paraoxon could be attributed to pi-pi stacking involving amino acid residues, Trp341 and Trp124. Conclusion: This study provided an insight of the molecular interaction of mangiferin with the studied enzymes and can be considered as a valuable tool for designing new drugs for better management of these diseases.en10.2174/1573406413666170307163929info:eu-repo/semantics/closedAccessAphloia theiformisdiabetes type 2mangiferinmolecular dockingnatural enzyme inhibitorobesityArticle13763364028290249Q3WOS:000414012200004Q3