In vitro and in silico Studies of Mangiferin from Aphloia theiformis on Key Enzymes Linked to Diabetes Type 2 and Associated Complications

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dc.contributor.authorPicot, Marie C. N.
dc.contributor.authorZengin, Gökhan
dc.contributor.authorMollica, Adriano
dc.contributor.authorStefanucci, Azzurra
dc.contributor.authorCarradori, Simone
dc.contributor.authorMahomoodally, Mohamad F.
dc.date.accessioned2020-03-26T19:41:53Z
dc.date.available2020-03-26T19:41:53Z
dc.date.issued2017
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractBackground: 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.en_US
dc.description.sponsorshipUniversity of Mauritius; University "G. d'Annunzio" of Chieti-Pescaraen_US
dc.description.sponsorshipThe authors gratefully acknowledge the University of Mauritius and University "G. d'Annunzio" of Chieti-Pescara for providing necessary support.en_US
dc.identifier.doi10.2174/1573406413666170307163929en_US
dc.identifier.endpage640en_US
dc.identifier.issn1573-4064en_US
dc.identifier.issn1875-6638en_US
dc.identifier.issue7en_US
dc.identifier.pmid28290249en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage633en_US
dc.identifier.urihttps://dx.doi.org/10.2174/1573406413666170307163929
dc.identifier.urihttps://hdl.handle.net/20.500.12395/35198
dc.identifier.volume13en_US
dc.identifier.wosWOS:000414012200004en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherBENTHAM SCIENCE PUBL LTDen_US
dc.relation.ispartofMEDICINAL CHEMISTRYen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectAphloia theiformisen_US
dc.subjectdiabetes type 2en_US
dc.subjectmangiferinen_US
dc.subjectmolecular dockingen_US
dc.subjectnatural enzyme inhibitoren_US
dc.subjectobesityen_US
dc.titleIn vitro and in silico Studies of Mangiferin from Aphloia theiformis on Key Enzymes Linked to Diabetes Type 2 and Associated Complicationsen_US
dc.typeArticleen_US

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