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Paper
Soft Matter, 2007, 3, 1401 - 1406, DOI: 10.1039/b709889h
Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent
M. J. Krysmann, V. Castelletto and I. W. Hamley
The self-assembly of a hydrophobically modified fragment of the amyloid
(A) peptide has been studied in methanol. The peptide FFKLVFF is based on A(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 -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 peptide and CD point to the importance of aromatic interactions between phenylalanine groups in driving aggregation into -sheets. The CD spectrum differs from that usually observed for -sheet assemblies formed by larger peptides or proteins and this is discussed for solutions in methanol and also trifluoroethanol. The fibril structure is imaged by transmission electron microscopy and scanning electron microscopy on dried samples and is confirmed by small-angle X-ray scattering experiments in solution.
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