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Influence of salt on the self-assembly of two model amyloid heptapeptides

Castelletto, V., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Cenker, C. and Olsson, U. (2010) Influence of salt on the self-assembly of two model amyloid heptapeptides. Journal of Physical Chemistry B, 114 (23). pp. 8002-8008. ISSN 1520-6106

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To link to this item DOI: 10.1021/jp102744g

Abstract/Summary

We study the effects of NaCl on the self-assembly of AAKLVFF and beta A beta AKLVFF in solution. Both AAKLVFF and beta A beta AKLVFF self-assemble into twisted fibers in aqueous solution. The addition of NaCl to aqueous solutions of AAKLVFF produces large crystal-like nanotapes which eventually precipitate. In contrast, highly twisted fibrils were observed for beta A beta AKLVFF solutions at low salt concentration, while a coexistence of highly twisted fibers and nanotubes was observed for beta A beta AKLVFF at high salt concentration. The self-assembled structures observed for beta A beta AKLVFF in NaCl solutions were ascribed to the progressive screening of the beta A beta AKLVFF surface charge caused by the addition of salt.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:16474
Publisher:American Chemical Society

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