@article{2959204,
    title = "Self-assembly of a model amphiphilic oligopeptide incorporating an arginine headgroup",
    author = "Ian W. Hamley and Ashkan Dehsorkhi and Valeria Castelletto and Jani Seitsonen and Janne Ruokolainen and Hermis Iatrou",
    journal = "Soft Matter",
    year = "2013",
    volume = "9",
    number = "19",
    pages = "4794",
    publisher = "Royal Society of Chemistry (RSC)",
    issn = "1744-683X, 1744-6848",
    doi = "10.1039/c3sm50303h",
    keywords = "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",
    abstract = "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."
}