publication . Article . 2007

Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent

M. J. Krysmann; V. Castelletto; I. W. Hamley;
Open Access English
  • Published: 17 Sep 2007
  • Publisher: Royal Society of Chemistry
  • Country: United Kingdom
Abstract
The self-assembly of a hydrophobically modified fragment of the amyloid beta(A beta) peptide has been studied in methanol. The peptide FFKLVFF is based on A beta(16-20) extended at the N terminus by two phenylalanine residues. The formation of amyloid-type fibrils is confirmed by Congo Red staining, thioflavin T fluorescence and circular dichroism experiments. FTIR points to the formation of beta-sheet structures in solution and in dried films and suggests that aggregation occurs at low concentration and is not strongly affected by further increase in concentration, i.e. the peptide is a strong fibril-former in methanol. UV fluorescence experiments on unstained ...
Subjects
free text keywords: Circular dichroism, Amyloid, Solvent, Phenylalanine, Fibril, Peptide, chemistry.chemical_classification, chemistry, Organic chemistry, Thioflavin, chemistry.chemical_compound, Fluorescence, Chromatography
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