Marie C.N. Picot*, Gokhan Zengin, Adriano Mollica, Azzurra Stefanucci, Simone Carradori and Mohamad F. Mahomoodally* Pages 633 - 640 ( 8 )
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 α-amylase, α-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 π-π and hydrogen bonds mostly. Mangiferin was docked to both allosteric and orthosteric sites of α-glucosidase by π-π 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 π-π 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.
Aphloia theiformis, diabetes type 2, mangiferin, molecular docking, natural enzyme inhibitor, obesity.
Department of Health Sciences, Faculty of Science, University of Mauritius, 230 Reduit, Department of Biology, Science Faculty, Selcuk University, Campus, 42250 Konya, Department of Pharmacy, University “G. d'Annunzio” of Chieti-Pescara, 66100, Chieti, Department of Pharmacy, University “G. d'Annunzio” of Chieti-Pescara, 66100, Chieti, Department of Pharmacy, University “G. d'Annunzio” of Chieti-Pescara, 66100, Chieti, Department of Health Sciences, Faculty of Science, University of Mauritius, 230 Reduit