SummaryA synthetic adhesion protein was designed by chemical grafting of the RGD tailed cyclic peptide cyclo[-D-Val-ArgGly-Asp-Glu(-EAhx-Tyr-Cys-NH~)-] 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.
This paper discusses the application of a method developed for cyclic peptide synthesis using allyl-based sidechain-protecting groups to obtain a so-called tailed cyclic peptide, a cyclic peptide bearing a side-chain anchoring tail. The method used for the synthesis ofcyclo[-D-Val-Arg-Gly-Asp-Asp(-eAhx-Cys-NH2)-] incorporates the c~-allylprotected aspartic acid Fmoc-L-Asp-OA1. A major side reaction, resulting in aspartimide formation, was observed when Fmoc-L-Asp-OA1 was incorporated into the sequence at the N-terminus of 6-aminohexanoic acid (eAhx). This side reaction leads to an aspartimidyl linear peptide with the same molecular weight as the expected cyclized peptide. Additionally, the undesired peptide contains a free amino terminus, which was responsible for further side reactions during the subsequent steps of the synthesis, mainly tetramethylguanidinium formation (M + 98) in TBTUinduced cyclization, and acetylation (M +42).
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.