Influence of salt on the self-assembly of two model amyloid heptapeptidesCastelletto, 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 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1021/jp102744g Abstract/SummaryWe 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.
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