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Self-assembly of a model amphiphilic oligopeptide incorporating an arginine headgroup

Hamley, I. W. ORCID:, Dehsorkhi, A., Castelletto, V., Seitsonen, J., Ruokolainen, J. and Iatrou, H. (2013) Self-assembly of a model amphiphilic oligopeptide incorporating an arginine headgroup. Soft Matter, 9 (19). pp. 4794-4801. ISSN 1744-683X

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To link to this item DOI: 10.1039/C3SM50303H


The self-assembly in aqueous solution of the alanine-rich peptide A12R2 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 A12R2 dimers. The packing of the alanine residues leads to distinct “b-sheet” spacings compared to those for amyloid-forming peptides. For this peptide, b-sheet structure coexists with some a-helical content. These ultrafine amyloid fibrils present arginine at high density on their surfaces, and this may lead to applications in nanobiotechnology.

Item Type:Article
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:32313
Publisher:Royal Society of Chemistry


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