TY - JOUR
TI - Self-assembly of a model amphiphilic oligopeptide incorporating an arginine headgroup
AU - Ian W. Hamley
AU - Ashkan Dehsorkhi
AU - Valeria Castelletto
AU - Jani Seitsonen
AU - Janne Ruokolainen
AU - Hermis Iatrou
JO - Soft Matter
PY - 2013
VL - 9
TODO - 19
SP - 4794
PB - Royal Society of Chemistry (RSC)
SN - 1744-683X, 1744-6848
TODO - 10.1039/c3sm50303h
TODO - Alanine residues;  Alanine-rich peptides;  Amyloid fibril;  Arginine residue;  Helical content;  Sheet structure;  Surfactant-like peptides;  Twisted tapes, Arginine;  Glycoproteins;  Oligomers;  Self assembly;  Transmission electron microscopy, Peptides
TODO - The self-assembly in aqueous solution of the alanine-rich peptide A 12R2 containing twelve alanine residues and two arginine residues has been investigated. This oligomeric peptide was synthesized via NCA-polymerization methods. The surfactant-like peptide is found via FTIR to form antiparallel dimers which aggregate into twisted fibrils, as revealed by cryogenic-transmission electron microscopy. The fibril substructure is probed via detailed X-ray scattering experiments, and are uniquely comprised of twisted tapes only 5 nm wide, set by the width of the antiparallel A12R 2 dimers. The packing of the alanine residues leads to distinct "β-sheet" spacings compared to those for amyloid-forming peptides. For this peptide, β-sheet structure coexists with some α-helical content. These ultrafine amyloid fibrils present arginine at high density on their surfaces, and this may lead to applications in nanobiotechnology. © 2013 The Royal Society of Chemistry.
ER -