Inhibitory effect of Zn2+ on α-glucosidase: Inhibition kinetics and molecular dynamics simulation

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dc.contributor.authorY F Zeng-
dc.contributor.authorJinhyuk Lee-
dc.contributor.authorY X Si-
dc.contributor.authorL Yan-
dc.contributor.authorT R Kim-
dc.contributor.authorG Y Qian-
dc.contributor.authorZ R Lu-
dc.contributor.authorZ M Ye-
dc.contributor.authorS J Yin-
dc.date.accessioned2017-04-19T09:36:00Z-
dc.date.available2017-04-19T09:36:00Z-
dc.date.issued2012-
dc.identifier.issn00329592-
dc.identifier.uri10.1016/j.procbio.2012.10.014ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11118-
dc.description.abstractα-Glucosidase (EC 3.2.1.20) is a critical enzyme with clinical relevance to type 2 diabetes mellitus. Therefore, research on this enzyme's inhibition is important. In the present study, we investigated Zn 2+-induced inhibition and the structural changes of α-glucosidase. α-Glucosidase activity was significantly inhibited by Zn2+ in a dose-dependent manner. The inhibition followed a multi-phase kinetic process with a first-order reaction. Zn2+ inhibited α-glucosidase in a parabolic mixed-type reaction (Ki = 0.102 ± 0.001 mM) and directly induced the unfolding of α-glucosidase, resulting in a slight hydrophobic exposure. We also performed 10 ns molecular dynamics simulations on α-glucosidase and Zn2+. The simulations suggest that ten Zn2+ ions possibly interact with 57 α-glucosidase residues. The molecular dynamics simulations also confirmed the binding mechanism of Zn2+ to α-glucosidase and suggest that the Zn2+ binding sites are not located in the glucose binding pocket of α-glucosidase. Our study provides insights into the mechanism of Zn2+-induced unfolding of α-glucosidase and inhibition of ligand binding and suggests that Zn 2+ could act as a potent inhibitor of α-glucosidase for the treatment of type 2 diabetes mellitus.-
dc.publisherElsevier-
dc.titleInhibitory effect of Zn2+ on α-glucosidase: Inhibition kinetics and molecular dynamics simulation-
dc.title.alternativeInhibitory effect of Zn2+ on α-glucosidase: Inhibition kinetics and molecular dynamics simulation-
dc.typeArticle-
dc.citation.titleProcess Biochemistry-
dc.citation.number12-
dc.citation.endPage2517-
dc.citation.startPage2510-
dc.citation.volume47-
dc.contributor.affiliatedAuthorJinhyuk Lee-
dc.contributor.alternativeNameZeng-
dc.contributor.alternativeName이진혁-
dc.contributor.alternativeNameSi-
dc.contributor.alternativeNameYan-
dc.contributor.alternativeName김태래-
dc.contributor.alternativeNameQian-
dc.contributor.alternativeNameLu-
dc.contributor.alternativeNameYe-
dc.contributor.alternativeNameYin-
dc.identifier.bibliographicCitationProcess Biochemistry, vol. 47, no. 12, pp. 2510-2517-
dc.identifier.doi10.1016/j.procbio.2012.10.014-
dc.subject.keywordα-Glucosidase-
dc.subject.keywordInhibition kinetics-
dc.subject.keywordMolecular dynamics-
dc.subject.keywordUnfolding-
dc.subject.keywordZn2+-
dc.subject.localα-Glucosidase-
dc.subject.localInhibition kinetics-
dc.subject.localMolecular dynamics-
dc.subject.localUnfolding-
dc.subject.localZn2+-
dc.description.journalClassY-
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Division of Biomedical Research > Genome Editing Research Center > 1. Journal Articles
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