Amyloid-? adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation.
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ABSTRACT:
SUBMITTER: Korshavn KJ
PROVIDER: S-EPMC4703560 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Publications
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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