Journal
SOFT MATTER
Volume 7, Issue 4, Pages 1326-1333Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c0sm00408a
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Funding
- EPSRC [EP/F048114/1, EP/G026203/1]
- Engineering and Physical Sciences Research Council [EP/F048114/1, EP/G026203/1] Funding Source: researchfish
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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 beta-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.
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