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Self-assembly of peptide nanotubes in an organic solvent

By M.J. Krysmann, V. Castelletto, J.E. McKendrick, L.A. Clifton, I.W. Hamley, P.J.F. Harris and S.A. King

Abstract

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

Publisher: American Chemical Society
Year: 2008
OAI identifier: oai:centaur.reading.ac.uk:11410
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