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Issue 4, 2011
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Hydrogelation of self-assembling RGD-based peptides

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Abstract

The self-assembly of tripeptides based on the RGD cell adhesion motif is investigated. Two tripeptides containing the Fmoc [N-(fluorenyl)-9-methoxycarbonyl] aromatic unit were synthesized, Fmoc-RGD and a control peptide containing a scrambled sequence, Fmoc-GRD. The Fmoc is used to control self-assembly via aromatic stacking interactions. The self-assembly and hydrogelation properties of the two Fmoc-tripeptides are compared. Both form well defined amyloid fibrils (as shown by cryo-TEM and SAXS) with β-sheet features in their circular dichroism and FTIR spectra. Both peptides form self-supporting hydrogels, the dynamic shear modulus of which was measured. Preliminary cell culture experiments reveal that Fmoc-RGD can be used as a support for bovine fibroblasts, but not Fmoc-GRD, consistent with the incorporation of the cell adhesion motif in the former peptide.

Graphical abstract: Hydrogelation of self-assembling RGD-based peptides

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Article information


Submitted
21 May 2010
Accepted
23 Jul 2010
First published
26 Aug 2010

Soft Matter, 2011,7, 1326-1333
Article type
Paper

Hydrogelation of self-assembling RGD-based peptides

G. Cheng, V. Castelletto, R. R. Jones, C. J. Connon and I. W. Hamley, Soft Matter, 2011, 7, 1326
DOI: 10.1039/C0SM00408A

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