Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance upgrade on Thursday 4th of May 2017 from 8.00am to 9.00am (BST).

During this time our websites will be offline temporarily. If you have any questions please use the feedback button on this page. We apologise for any inconvenience this might cause and thank you for your patience.


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
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 17 Oct 2015, accepted on 06 Nov 2015 and first published on 06 Nov 2015


Article type: Communication
DOI: 10.1039/C5CC08634E
Citation: Chem. Commun., 2016,52, 882-885
  •   Request permissions

    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

Search articles by author