Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95431
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dc.contributor.authorZhang, Yunen
dc.contributor.authorLuo, Yinen
dc.contributor.authorDeng, Yonghuaen
dc.contributor.authorMu, Yuguangen
dc.contributor.authorWei, Guanghongen
dc.date.accessioned2013-02-27T07:26:24Zen
dc.date.accessioned2019-12-06T19:14:43Z-
dc.date.available2013-02-27T07:26:24Zen
dc.date.available2019-12-06T19:14:43Z-
dc.date.copyright2012en
dc.date.issued2012en
dc.identifier.citationZhang, Y., Luo, Y., Deng, Y., Mu, Y., & Wei, G. (2012). Lipid Interaction and Membrane Perturbation of Human Islet Amyloid Polypeptide Monomer and Dimer by Molecular Dynamics Simulations. PLoS ONE, 7(5).en
dc.identifier.issn1932-6203en
dc.identifier.urihttps://hdl.handle.net/10356/95431-
dc.identifier.urihttp://hdl.handle.net/10220/9294en
dc.description.abstractThe aggregation of human islet amyloid polypeptide (hIAPP or amylin) is associated with the pathogenesis of type 2 diabetes mellitus. Increasing evidence suggests that the interaction of hIAPP with β-cell membranes plays a crucial role in cytotoxicity. However, the hIAPP-lipid interaction and subsequent membrane perturbation is not well understood at atomic level. In this study, as a first step to gain insight into the mechanism of hIAPP-induced cytotoxicity, we have investigated the detailed interactions of hIAPP monomer and dimer with anionic palmitoyloleolyophosphatidylglycerol (POPG) bilayer using all-atom molecular dynamics (MD) simulations. Multiple MD simulations have been performed by employing the initial configurations where the N-terminal region of hIAPP is pre-inserted in POPG bilayer. Our simulations show that electrostatic interaction between hIAPP and POPG bilayer plays a major role in peptide-lipid interaction. In particular, the N-terminal positively-charged residues Lys1 and Arg11 make a dominant contribution to the interaction. During peptide-lipid interaction process, peptide dimerization occurs mostly through the C-terminal 20–37 region containing the amyloidogenic 20–29-residue segment. Membrane-bound hIAPP dimers display a pronounced ability of membrane perturbation than monomers. The higher bilayer perturbation propensity of hIAPP dimer likely results from the cooperativity of the peptide-peptide interaction (or peptide aggregation). This study provides insight into the hIAPP-membrane interaction and the molecular mechanism of membrane disruption by hIAPP oligomers.en
dc.language.isoenen
dc.relation.ispartofseriesPLoS oNEen
dc.rights© 2012 The Authors.en
dc.titleLipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulationsen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0038191en
dc.description.versionPublished versionen
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