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
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