Peptide-synthetic polymer conjugates have received a growing interest for several years, because of their applications not only in biological areas such as drug delivery and tissue engineering, but also in nanotechnology area. Design of materials that are capable of effectively mimicking bioactive surface relies on controlled synthesis techniques. Significant progress in developing such techniques has been made in polymer chemistry, and a number of methods are currently available for preparing materials with defined molecular architecture.

The Arg-Gly-Asp-Ser(RGDS) sequence is a cell-adhesion motif present in several matrixes associated with adhesive glycoproteins including fibronectin. The RGDS sequence is recognized by several integrins, including those on the surface of the platelet and fibroblast cells. In this work, we aimed to improve the biological activity of the silica surface, and thereby selected the cationic polymer poly(4-vinylpyridine)(P4VP) and the RGDS peptide derived from fibronectin cell-attachment protein to conjugate them into a peptide-synthetic polymer. We synthesized 4,4’-azobis(4-cyanovalericacid)(ACVA), an initiator of radical polymerization, and attached it to GRGDS peptide. P4VP-Peptide was polymerized from the peptides that included the initiator. P4VP-Peptide was applied onto the silica surface and evaluated by X-ray photoelectron spectroscopy, surface plasmon resonance and contact angle measurements. The cell-attachment activity was assessed by cell-attachment assay of L929 cell binding to peptide-immobilized silica surface.

P4VP and P4VP-Peptide were adsorbed onto silica surface. P4VP-Peptide had a higher cell attachment activity than P4VP and the non-coated glass plate. Our data show that the P4VP-Peptide displays promising results for a new organic-inorganic biomaterial.