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- W2656340138 endingPage "9575" @default.
- W2656340138 startingPage "9566" @default.
- W2656340138 abstract "Previously published experimental studies have suggested that when the 40-residue amyloid beta peptide is encapsulated in a reverse micelle, it folds into a structure that may nucleate amyloid fibril formation (Yeung, P. S.-W.; Axelsen, P. H. J. Am. Chem. Soc. 2012, 134, 6061 ). The factors that induce the formation of this structure have now been identified in a multi-microsecond simulation of the same reverse micelle system that was studied experimentally. Key features of the polypeptide-micelle interaction include the anchoring of a hydrophobic residue cluster into gaps in the reverse micelle surface, the formation of a beta turn at the anchor point that brings N- and C-terminal segments of the polypeptide into proximity, high ionic strength that promotes intramolecular hydrogen bond formation, and deformation of the reverse micelle surface to facilitate interactions with the surface along the entire length of the polypeptide. Together, these features cause the simulation-derived vibrational spectrum to red shift in a manner that reproduces the red-shift previously reported experimentally. On the basis of these findings, a new mechanism is proposed whereby membranes nucleate fibril formation and facilitate the in-register alignment of polypeptide strands that is characteristic of amyloid fibrils." @default.
- W2656340138 created "2017-06-30" @default.
- W2656340138 creator A5011627095 @default.
- W2656340138 creator A5085858278 @default.
- W2656340138 date "2017-07-05" @default.
- W2656340138 modified "2023-10-14" @default.
- W2656340138 title "Amyloid Beta Peptide Folding in Reverse Micelles" @default.
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- W2656340138 doi "https://doi.org/10.1021/jacs.7b03333" @default.
- W2656340138 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28631483" @default.
- W2656340138 hasPublicationYear "2017" @default.
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