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

We study the effects of NaCl on the self-assembly of AAKLVFF and βAβAKLVFF in solution. Both AAKLVFF and βAβAKLVFF 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 contra...

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Bibliographic Details
Published inThe journal of physical chemistry. B Vol. 114; no. 23; pp. 8002 - 8008
Main Authors Castelletto, V, Hamley, I.W, Cenker, C, Olsson, U
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 17.06.2010
Subjects
Amino Acid Sequence
Amyloid beta-Peptides - chemistry
B: Biophysical Chemistry
Chemical Sciences
Circular Dichroism
Fysikalisk kemi
Kemi
Nanotubes - chemistry
Nanotubes - ultrastructure
Natural Sciences
Naturvetenskap
Peptides - chemistry
Physical Chemistry
Protein Structure, Secondary
Sodium Chloride - chemistry
Spectroscopy, Fourier Transform Infrared
Water - chemistry
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Summary:We study the effects of NaCl on the self-assembly of AAKLVFF and βAβAKLVFF in solution. Both AAKLVFF and βAβAKLVFF 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 βAβAKLVFF solutions at low salt concentration, while a coexistence of highly twisted fibers and nanotubes was observed for βAβAKLVFF at high salt concentration. The self-assembled structures observed for βAβAKLVFF in NaCl solutions were ascribed to the progressive screening of the βAβAKLVFF surface charge caused by the addition of salt.
Bibliography:ObjectType-Article-1
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content type line 23
ISSN:1520-6106
1520-5207
1520-5207
DOI:10.1021/jp102744g