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Issue 5, 2016
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Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation

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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

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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
Author version available: Download Author version (PDF)
Citation: Chem. Commun., 2016,52, 882-885
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    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

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