title: In vitro and in silico Studies of Mangiferin from Aphloia theiformis on Key Enzymes Linked to Diabetes Type 2 and Associated Complications.
abstract: 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.
  
  
  METHODS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Health Sciences, Faculty of Science, University of Mauritius, 230 Reduit. Mauritius.
authors.forename: Marie C N
authors.initials: MCN
authors.lastname: Picot
authors.affiliation: Department of Biology, Science Faculty, Selcuk University, Campus, 42250 Konya. Turkey.
authors.forename: Gokhan
authors.initials: G
authors.lastname: Zengin
authors.affiliation: Department of Pharmacy, University "G. d'Annunzio" of Chieti-Pescara, 66100, Chieti. Italy.
authors.forename: Adriano
authors.initials: A
authors.lastname: Mollica
authors.affiliation: Department of Pharmacy, University "G. d'Annunzio" of Chieti-Pescara, 66100, Chieti. Italy.
authors.forename: Azzurra
authors.initials: A
authors.lastname: Stefanucci
authors.affiliation: Department of Pharmacy, University "G. d'Annunzio" of Chieti-Pescara, 66100, Chieti. Italy.
authors.forename: Simone
authors.initials: S
authors.lastname: Carradori
authors.affiliation: Department of Health Sciences, Faculty of Science, University of Mauritius, 230 Reduit. Mauritius.
authors.forename: Mohamad F
authors.initials: MF
authors.lastname: Mahomoodally
mesh_terms: D000495:Allosteric Site; D000818:Animals; D020134:Catalytic Domain; D003924:Diabetes Mellitus, Type 2 / Q000201:enzymology*; D007887:Fabaceae; D024981:Glycogen Phosphorylase / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D006867:Hydrolases / Q000737:chemistry*; D007700:Kinetics; D062105:Molecular Docking Simulation; D010261:Paraoxon / Q000737:chemistry; D013552:Swine; D064028:Tracheophyta / Q000737:chemistry; D044004:Xanthones / Q000737:chemistry*
chemical_list: D044004:Xanthones; C013592:mangiferin; D024981:Glycogen Phosphorylase; D006867:Hydrolases; D010261:Paraoxon
keywords: Aphloia theiformis; diabetes type 2; mangiferin; molecular docking; natural enzyme inhibitor; obesity