Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation
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- Title
- Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation
- Author
- Lim, Mi Hee; Korshavn, Kyle J.; Ramamoorthy, Ayyalusamy; Bhunia, Anirban
- Issue Date
- 2016-01
- Publisher
- ROYAL SOC CHEMISTRY
- 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).
- URI
- https://scholarworks.unist.ac.kr/handle/201301/18092
- URL
- http://pubs.rsc.org/en/Content/ArticleLanding/2015/CC/C5CC08634E#!divAbstract
- DOI
- 10.1039/C5CC08634E
- ISSN
- 1359-7345
- Appears in Collections:
- PHY_Journal Papers
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