Jump to main content
Jump to site search

Issue 5, 2016
Previous Article Next Article

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

Author affiliations

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).

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

Back to tab navigation

Supplementary files

Article information


Submitted
17 Oct 2015
Accepted
06 Nov 2015
First published
06 Nov 2015

Chem. Commun., 2016,52, 882-885
Article type
Communication
Author version available

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

K. J. Korshavn, A. Bhunia, M. H. Lim and A. Ramamoorthy, Chem. Commun., 2016, 52, 882
DOI: 10.1039/C5CC08634E

Social activity

Search articles by author

Spotlight

Advertisements