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Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation

Author(s)
Lim, Mi HeeKorshavn, Kyle J.Ramamoorthy, AyyalusamyBhunia, Anirban
Issued Date
2016-01
DOI
10.1039/C5CC08634E
URI
https://scholarworks.unist.ac.kr/handle/201301/18092
Fulltext
http://pubs.rsc.org/en/Content/ArticleLanding/2015/CC/C5CC08634E#!divAbstract
Citation
CHEMICAL COMMUNICATIONS, v.52, no.5, pp.882 - 885
Abstract
Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β (Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of Aβ40 on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22).
Publisher
ROYAL SOC CHEMISTRY
ISSN
1359-7345
Keyword
ALZHEIMERS-DISEASENMR-SPECTROSCOPYA-BETAPEPTIDEAGGREGATIONRESOLUTIONMECHANISMFIBRILSSTATES

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