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Chirality effects at each amino acid position on tripeptide self-assembly into hydrogel biomaterials.

Authors
  • Marchesan, S
  • Easton, C D
  • Styan, K E
  • Waddington, L J
  • Kushkaki, F
  • Goodall, L
  • McLean, K M
  • Forsythe, J S
  • Hartley, P G
Type
Published Article
Journal
Nanoscale
Publisher
The Royal Society of Chemistry
Publication Date
May 21, 2014
Volume
6
Issue
10
Pages
5172–5180
Identifiers
DOI: 10.1039/c3nr06752a
PMID: 24700146
Source
Medline
License
Unknown

Abstract

Hydrogels formed by ultrashort peptides are emerging as cost-effective materials for cell culture. However, L-peptides are labile to proteases, while their D-isomers are thought to not support cell growth as well. In contrast, the self-assembly behaviour and biological performance of heterochiral peptides (i.e., made of both d and l amino acids) are largely unknown. In this study, we evaluate the effects of amino acid chirality on tripeptide self-assembly and hydrogelation at physiological pH, and cytocompatibility in fibroblast cell culture. A series of uncapped hydrophobic tripeptides with all combinations of d, l amino acids was prepared, tested for self-assembly under physiological conditions, and analysed by circular dichroism, FT-IR, cryo-TEM, AFM, and Thioflavin T fluorescence imaging. Amino acid chirality has a profound effect on the peptides' supramolecular behaviour. Only selected isomers form hydrogels, and of amyloid structure, as confirmed by rheology and XRD. Importantly, they are able to maintain the viability and proliferation of fibroblasts in vitro. This study identifies two heterochiral gels that perform well in cell culture and will assist in the design of innovative and cost-effective peptide gel biomaterials.

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