Fibroblast attachment to Arg-Gly-Asp peptide-immobilized poly(gamma-methyl L-glutamate).

The attachment of MRC-5 human fibroblasts was investigated on poly(gamma-methyl L-glutamate) (PMLG), and upon cell adhesion peptides Arg-Gly-Asp-Ser (RGDS)- and Gly-Arg-Gly-Asp-Ser (GRGDS)-immobilized PMLG (RGDS-PMLG and GRGDS-PMLG). The peptides were immobilized by their N-terminal amine to activated PMLG surfaces. Prior to peptide immobilization, the aminolysis of PMLG surfaces was performed with hydrazine hydrate (HA), ethylenediamine (EDA), and hexamethylenediamine (HMDA) and was followed by the activation with hexamethylene diisocyanate. Surface characterization of these films was carried out by means of a Fourier transform IR (FT-IR) spectrometer equipped with an attenuated total reflectance (ATR) attachment. The amount of immobilized RGDS could be controlled by the reaction time of the aminolysis. The effects of HA, EDA, and HMDA as a spacer on the cell attachment were also investigated, and it was suggested that a longer spacer promoted the cell attachment via specific receptor-ligand interaction.