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Issue 9, 2011
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Self-assembly of amphiphilic peptides

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The self-assembly of amphiphilic peptides is reviewed. The review covers surfactant-like peptides with amphiphilicity arising from the sequence of natural amino acids, and also peptide amphiphiles (PAs) in which lipid chains are attached to hydrophilic peptide sequences containing charged residues. The influence of the secondary structure on the self-assembled structure and vice versa is discussed. For surfactant-like peptides structures including fibrils, nanotubes, micelles and vesicles have been reported. A particularly common motif for PAs is β-sheet based fibrils, although other structures have been observed. In these structures, the peptide epitope is presented at the surface of the nanostructure, providing remarkable bioactivity. Recent discoveries of potential, and actual, applications of these materials in biomedicine and bionanotechnology are discussed.

Graphical abstract: Self-assembly of amphiphilic peptides

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Publication details

The article was received on 27 Oct 2010, accepted on 26 Jan 2011 and first published on 16 Feb 2011

Article type: Tutorial Review
DOI: 10.1039/C0SM01218A
Citation: Soft Matter, 2011,7, 4122-4138

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    Self-assembly of amphiphilic peptides

    I. W. Hamley, Soft Matter, 2011, 7, 4122
    DOI: 10.1039/C0SM01218A

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