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1. Zhang Y, Luo Y, Deng Y, Mu Y, Wei G: Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations. PLoS One; 2012;7(5):e38191

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.
  • 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.
  • [MeSH-major] Cell Membrane / metabolism. Islet Amyloid Polypeptide / chemistry. Islet Amyloid Polypeptide / metabolism. Lipid Metabolism. Molecular Dynamics Simulation. Protein Multimerization
  • [MeSH-minor] Amino Acid Sequence. Humans. Lipid Bilayers / chemistry. Lipid Bilayers / metabolism. Molecular Sequence Data. Peptide Fragments / chemistry. Peptide Fragments / metabolism. Phosphatidylcholines / metabolism. Protein Structure, Secondary. Solvents / chemistry. Static Electricity

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  • (PMID = 22693597.001).
  • [ISSN] 1932-6203
  • [Journal-full-title] PloS one
  • [ISO-abbreviation] PLoS ONE
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Islet Amyloid Polypeptide; 0 / Lipid Bilayers; 0 / Peptide Fragments; 0 / Phosphatidylcholines; 0 / Solvents; TE895536Y5 / 1-palmitoyl-2-oleoylphosphatidylcholine
  • [Other-IDs] NLM/ PMC3364971
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