Journal
SOFT MATTER
Volume 9, Issue 19, Pages 4794-4801Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3sm50303h
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Funding
- European Soft Matter Infrastructure Initiative (ESMI) [S110700102]
- EPSRC [EP/G026203/1, EP/G067538/1]
- ESRF [SC3468, MX-1401]
- Engineering and Physical Sciences Research Council [EP/G067538/1, EP/G026203/1] Funding Source: researchfish
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The self-assembly in aqueous solution of the alanine-rich peptide A(12)R(2) 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 A(12)R(2) dimers. The packing of the alanine residues leads to distinct beta-sheet spacings compared to those for amyloid-forming peptides. For this peptide, beta-sheet structure coexists with some alpha-helical content. These ultrafine amyloid fibrils present arginine at high density on their surfaces, and this may lead to applications in nanobiotechnology.
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