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