Self-assembly of peptide nanotubes in an organic solvent
Krysmann, M.J., Castelletto, V., McKendrick, J.E., Clifton, L.A., Hamley, I.W., Harris, P.J.F. and King, S.A. (2008) Self-assembly of peptide nanotubes in an organic solvent. Langmuir, 24 (15). pp. 8158-8162. ISSN 0743-7463
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To link to this article DOI: 10.1021/la800942n
The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence A beta(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 beta-sheet self-assembly. The beta-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped beta-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.