Nag, Suman ; Sarkar, Bidyut ; Chandrakesan, Muralidharan ; Abhyanakar, Rajiv ; Bhowmik, Debanjan ; Kombrabail, Mamata ; Dandekar, Sucheta ; Lerner, Eitan ; Haas, Elisha ; Maiti, Sudipta (2013) A folding transition underlies the emergence of membrane affinity in amyloid-β Physical Chemistry Chemical Physics, 15 (44). pp. 19129-19133. ISSN 1463-9076
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Official URL: http://pubs.rsc.org/en/content/articlelanding/2013...
Related URL: http://dx.doi.org/10.1039/C3CP52732H
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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Royal Society of Chemistry. |
| ID Code: | 112973 |
| Deposited On: | 24 May 2018 11:23 |
| Last Modified: | 24 May 2018 11:23 |
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