Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/95431
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Zhang, Yun | en |
dc.contributor.author | Luo, Yin | en |
dc.contributor.author | Deng, Yonghua | en |
dc.contributor.author | Mu, Yuguang | en |
dc.contributor.author | Wei, Guanghong | en |
dc.date.accessioned | 2013-02-27T07:26:24Z | en |
dc.date.accessioned | 2019-12-06T19:14:43Z | - |
dc.date.available | 2013-02-27T07:26:24Z | en |
dc.date.available | 2019-12-06T19:14:43Z | - |
dc.date.copyright | 2012 | en |
dc.date.issued | 2012 | en |
dc.identifier.citation | Zhang, 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.issn | 1932-6203 | en |
dc.identifier.uri | https://hdl.handle.net/10356/95431 | - |
dc.description.abstract | The 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.iso | en | en |
dc.relation.ispartofseries | PLoS oNE | en |
dc.rights | © 2012 The Authors. | en |
dc.title | Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations | en |
dc.type | Journal Article | en |
dc.contributor.school | School of Biological Sciences | en |
dc.identifier.doi | 10.1371/journal.pone.0038191 | en |
dc.description.version | Published version | en |
dc.identifier.pmid | 22693597 | - |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
Appears in Collections: | SBS Journal Articles |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
18. Lipid Interaction and Membrane Perturbation.pdf | 756.13 kB | Adobe PDF | View/Open |
SCOPUSTM
Citations
10
40
Updated on Mar 23, 2024
Web of ScienceTM
Citations
5
62
Updated on Oct 26, 2023
Page view(s) 20
672
Updated on Mar 28, 2024
Download(s) 20
311
Updated on Mar 28, 2024
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.