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Cited by 435

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Self-assembly of amphiphilic peptides

Open access
Hamley, I. W.·2011·Soft Matter

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.

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Metadata

Authors
Hamley, I. W.
Venue
Soft Matter
Published
2011
Volume
7
Issue
9
Pages
4122
ISSN
  • 1744-683X (ISSN-L)
  • 1744-6848
OpenAlex
W1976915573
Cited by
435
References
3
FWCI
15.06
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Self-assembly of amphiphilic peptides. https://app.cochat.ai/papers/10.1039/c0sm01218a
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Hamley, I. W. (2011). Self-assembly of amphiphilic peptides. Soft Matter. https://doi.org/10.1039/c0sm01218a

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.