Picot_2017_Med.Chem_13_633

BACKGROUND: 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 alpha-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.