Self-assembly of peptide nanotubes in an organic solvent

Krysmann, M.J., Castelletto, V., McKendrick, J.E. ORCID: https://orcid.org/0000-0003-2275-0569, Clifton, L.A., Hamley, I.W. ORCID: https://orcid.org/0000-0002-4549-0926, 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 doi: 10.1021/la800942n

Abstract/Summary

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.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/11410
Item Type	Article
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) > Mass Spectrometry (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Uncontrolled Keywords	AMYLOID PEPTIDE, INTEGRAL-EQUATIONS, ALZHEIMERS-DISEASE, SPECTROSCOPY, FIBRILS, DIPHENYLALANINE, FIBRILLOGENESIS, NANOWIRES, FRAGMENT, RIBBONS
Publisher	American Chemical Society
Download/View statistics	View download statistics for this item