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- W2330221657 abstract "Disruption of the cellular membrane by the amyloidogenic peptide, islet amyloid polypeptide (IAPP), has been considered as one of the mechanisms of $ensuremath{beta}$-cell death during type 2 diabetes. The N-terminal region (residues 1--19) of the human version of IAPP is suggested to be primarily responsible for the membrane-disrupting effect of the full-length hIAPP peptide. However, the detailed assembly mode of hIAPP1--19 with membrane remains unclear. To gain insight into the interactions of hIAPP1--19 oligomer with the model membrane, we have employed coarse-grained molecular dynamics self-assembly simulations to study the aggregation of hIAPP1--19 fragments in the binary lipid made of zwitterionic dipalmitoylphosphatidylcholine (DPPC) and anionic dipalmitoylphosphatidylserine (DPPS) in the presence and absence of different levels of cholesterol content. The membrane-destabilizing effect of hIAPP1--19 is found to be modulated by the presence of cholesterol. In the absence of cholesterol, hIAPP1--19 aggregates prefer to locate inside the bilayer, forming pore-like assemblies. While in the presence of cholesterol molecules, the lipid bilayer becomes more ordered and stiff, and the hIAPP1--19 aggregates are dominantly positioned at the bilayer-water interface. The action of cholesterol may suggest a possible way to maintain the membrane integrity by small molecule interference." @default.
- W2330221657 created "2016-06-24" @default.
- W2330221657 creator A5007399260 @default.
- W2330221657 creator A5036968132 @default.
- W2330221657 creator A5037216734 @default.
- W2330221657 creator A5066791109 @default.
- W2330221657 creator A5071286986 @default.
- W2330221657 date "2011-11-29" @default.
- W2330221657 modified "2023-09-23" @default.
- W2330221657 title "Effects of cholesterol on pore formation in lipid bilayers induced by human islet amyloid polypeptide fragments: A coarse-grained molecular dynamics study" @default.
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- W2330221657 doi "https://doi.org/10.1103/physreve.84.051922" @default.