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

The Mina and Everard Goodman Faculty of Life Sciences - at Bar-Ilan University

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

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

All Science Journal Classification (ASJC) codes

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1039/c3cp52732h

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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.",

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

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AU - Nag, Suman

AU - Sarkar, Bidyut

AU - Chandrakesan, Muralidharan

AU - Abhyanakar, Rajiv

AU - Bhowmik, Debanjan

AU - Kombrabail, Mamata

AU - Dandekar, Sucheta

AU - Lerner, Eitan

AU - Haas, Elisha

AU - Maiti, Sudipta

PY - 2013/11/28

Y1 - 2013/11/28

N2 - 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.

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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DO - 10.1039/c3cp52732h

M3 - مقالة

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EP - 19133

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

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ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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