Accessibility navigation


Hydrogelation of self-assembling RGD-based peptides

Cheng, G., Castelletto, V., Jones, R. R., Connon, C. J. and Hamley, I. W. (2011) Hydrogelation of self-assembling RGD-based peptides. Soft Matter, 7 (4). pp. 1326-1333. ISSN 1744-683X

Full text not archived in this repository.

To link to this article DOI: 10.1039/C0SM00408A

Abstract/Summary

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 selfassembly 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 b-sheet features in their circular dichroism and FTIR spectra. Both peptides form selfsupporting 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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Division of Pharmacology
Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) > Electron Microscopy Laboratory (CAF)
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:18933
Publisher:Royal Society of Chemistry

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation