Self-assembly of Peptide nanotubes in an organic solvent.
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.
Department of Chemistry, University of Reading, Reading, UK.
M J
MJ
Krysmann
V
V
Castelletto
J E
JE
McKendrick
L A
LA
Clifton
I
I
W Hamley
P J F
PJ
Harris
S M
SM
King
D002942:Circular Dichroism; D000432:Methanol / Q000737:chemistry*; D046529:Microscopy, Electron, Transmission; D015394:Molecular Structure; D045333:Nanotubes, Peptide / Q000737:chemistry* / Q000648:ultrastructure; D012997:Solvents / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
D045333:Nanotubes, Peptide; D012997:Solvents; D000432:Methanol