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

doi:10.1039/c3cp52732h

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 journal › Article › peer-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 language	English
Pages (from-to)	19129-19133
Number of pages	5
Journal	Physical Chemistry Chemical Physics
Volume	15
Issue number	44
DOIs	https://doi.org/10.1039/c3cp52732h
State	Published - 28 Nov 2013
Externally published	Yes

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AU - Chandrakesan, Muralidharan

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AU - Bhowmik, Debanjan

AU - Kombrabail, Mamata

AU - Dandekar, Sucheta

AU - Lerner, Eitan

AU - Haas, Elisha

AU - Maiti, Sudipta

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AB - 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.

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

Abstract

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