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

Suman Nag, Bidyut Sarkar, Muralidharan Chandrakesan, Rajiv Abhyanakar, Debanjan Bhowmik, Mamata Kombrabail, Sucheta Dandekar, Eitan Lerner, Elisha Haas, Sudipta Maiti*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

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.

Original languageAmerican English
Pages (from-to)19129-19133
Number of pages5
JournalPhysical Chemistry Chemical Physics
Volume15
Issue number44
DOIs
StatePublished - 28 Nov 2013
Externally publishedYes

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