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- W1990468756 abstract "Several neurodegenerative diseases such as Alzheimer's and Parkinson's diseases as well as nonneuropathic diseases such as type II diabetes and atrial amyloidosis are associated with aggregation of amyloid polypeptides into fibrillar structures, or plaques. In this study, we use molecular dynamics simulations to test the stability and orientation of membrane-embedded aggregates of the human islet amyloid polypeptide (hIAPP) implicated in type II diabetes. We find that in both monolayers and bilayers of dipalmitoylphosphatidylglycerol (DPPG) hIAPP trimers and tetramers remain inside the membranes and preserve their β-sheet secondary structure. Lipid bilayer-inserted hIAPP trimers and tetramers orient inside DPPG at 60° relative to the membrane/water interface and lead to water permeation and Na(+) intrusion, consistent with ion-toxicity in islet β-cells. In particular, hIAPP trimers form a water-filled β-sandwich that induce water permeability comparable with channel-forming proteins, such as aquaporins and gramicidin-A. The predicted disruptive orientation is consistent with the amphiphilic properties of the hIAPP aggregates and could be probed by chiral sum frequency generation (SFG) spectroscopy, as predicted by the simulated SFG spectra." @default.
- W1990468756 created "2016-06-24" @default.
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- W1990468756 creator A5077352287 @default.
- W1990468756 creator A5089129603 @default.
- W1990468756 date "2013-11-01" @default.
- W1990468756 modified "2023-10-13" @default.
- W1990468756 title "Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides" @default.
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- W1990468756 doi "https://doi.org/10.1016/j.bpj.2013.09.045" @default.
- W1990468756 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3838749" @default.
- W1990468756 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24268144" @default.
- W1990468756 hasPublicationYear "2013" @default.
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