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Issue 44, 2013
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A folding transition underlies the emergence of membrane affinity in amyloid-β

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Abstract

Small amyloid-β (Aβ) oligomers have much higher membrane affinity compared to the monomers, but the structural origin of this functional change is not understood. We show that as monomers assemble into small n-mers (n < 10), Aβ acquires a tertiary fold that is consistent with the mature fibrils. This is an early and defining transition for the aggregating peptide, and possibly underpins its altered bioactivity.

Graphical abstract: A folding transition underlies the emergence of membrane affinity in amyloid-β

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Publication details

The article was received on 30 Jun 2013, accepted on 27 Sep 2013 and first published on 30 Sep 2013


Article type: Communication
DOI: 10.1039/C3CP52732H
Citation: Phys. Chem. Chem. Phys., 2013,15, 19129-19133

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    A folding transition underlies the emergence of membrane affinity in amyloid-β

    S. Nag, B. Sarkar, M. Chandrakesan, R. Abhyanakar, D. Bhowmik, M. Kombrabail, S. Dandekar, E. Lerner, E. Haas and S. Maiti, Phys. Chem. Chem. Phys., 2013, 15, 19129
    DOI: 10.1039/C3CP52732H

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