A synthetic adhesion protein was designed by chemical grafting of the RGD tailed cyclic peptide cyclo[-D-Val-Arg-Gly-Asp-Glu(-∈Ahx-Tyr-Cys-NH2)-] on the carrier protein bovine serum albumin (BSA). The cyclic conformation of the RGD motif grafted on the protein mimics the conformation of the motif displayed in native adhesion proteins such as fibronectin. The adhesion of the cells on polystyrene coated with the conjugate BSA-peptide was similar or even better than the one obtained when the proadhesive protein fibronectin was coated on the plates. Results also indicated that covalent coupling of the peptide on BSA is not absolutely required, since simple adsorption of the peptide on the protein coated on plates was efficient for enhancing cell adhesion. These results show that polystyrene support can be reconditioned with conformationally constrained RGD peptides to enhance cell adhesion on solid supports. The same methodology can be adapted for the development of new biomaterials based on the recognition of specific peptides.
|Pages (de - à)||87-91|
|Nombre de pages||5|
|journal||Letters in peptide science|
|Numéro de publication||2-3|
|Etat de la publication||Publié - 1998|