| Literature DB >> 18572891 |
M J Krysmann1, V Castelletto, J E McKendrick, L A Clifton, I W Hamley, P J F Harris, S M King.
Abstract
The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence Abeta(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.Entities:
Mesh:
Substances:
Year: 2008 PMID: 18572891 DOI: 10.1021/la800942n
Source DB: PubMed Journal: Langmuir ISSN: 0743-7463 Impact factor: 3.882