Self-assembly of amphiphilic peptides
Top Cited Papers
- 16 February 2011
- journal article
- review article
- Published by Royal Society of Chemistry (RSC) in Soft Matter
- Vol. 7 (9), 4122-4138
- https://doi.org/10.1039/c0sm01218a
Abstract
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.This publication has 100 references indexed in Scilit:
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