4.5 Article

Influence of Salt on the Self-Assembly of Two Model Amyloid Heptapeptides

Journal

JOURNAL OF PHYSICAL CHEMISTRY B
Volume 114, Issue 23, Pages 8002-8008

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jp102744g

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Funding

  1. Biocentre, University of Reading
  2. EPSRC [EP/G026203/1] Funding Source: UKRI

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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.

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