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Phys Chem Chem Phys. 2013 Nov 28;15(44):19129-33. doi: 10.1039/c3cp52732h.

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

Author information

  • 1Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India. maiti@tifr.res.in.

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.

PMID:
24121316
[PubMed - indexed for MEDLINE]
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