Self-Assembly of Peptide Nanotubes in an Organic Solvent

Krysmann, Marta orcid iconORCID: 0000-0002-8036-4925, Castelletto, V., McKendrick, J. E., Clifton, L.A., Hamley, I.W., Harrison, P.J.F. and King, S.M. (2008) Self-Assembly of Peptide Nanotubes in an Organic Solvent. Langmuir, 24 (15). pp. 8158-8162. ISSN 0743-7463

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The self-assembly of a modified fragment of the amyloid β peptide, based on sequence Aβ(16−20), KLVFF, extended to give AAKLVFF is studied in methanol. Self-assembly into peptide nanotubes is observed, as confirmed by electron microscopy and small-angle X-ray scattering. The secondary structure of the peptide is probed by FTIR and circular dichroism, and UV/visible spectroscopy provides evidence for the important role of aromatic interactions between phenylalanine residues in driving β-sheet self-assembly. The β-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped β-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.

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