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


ABSTRACT: Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-? (A?) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of A?40 on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22).

SUBMITTER: Korshavn KJ 

PROVIDER: S-EPMC4703560 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature

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

Korshavn Kyle J KJ   Bhunia Anirban A   Lim Mi Hee MH   Ramamoorthy Ayyalusamy A  

Chemical communications (Cambridge, England) 20160101 5


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). ...[more]

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