Chemical modification of metallic implant surfaces with biofunctional proteins (Part 1). Molecular structure and biological activity of a modified NiTi alloy surface.

Human plasma fibronectin (pFN), an adhesive protein, was covalently immobilized onto an alkylaminosilane derivative of a NiTi substrate with glutaraldehyde through Schiff's base formation. The surface at different stages of the modification was characterized by X-ray photoelectron spectroscopy (XPS), and the amount of immobilized pFN was determined by a fluorometric method. The spreading behavior of human gingival fibroblasts was examined on the modified surface. The XPS spectra suggested that gamma-aminopropyltriethoxysilane (gamma-APS) was bonded to the surface through metallosiloxane bonds (Ti-O-Si) formed via a condensation reaction between the silanol end of gamma-APS and the surface hydroxyl group, with a highly cross-linked siloxane network formed after heat treatment of the silanized surface at 100 degrees C. The pFN was immobilized at the surface density of 1.1 micrograms.cm-2, and significantly promoted fibroblast spreading, suggesting that this chemical modification offers an effective means of controlling metal/cell interactions. These results may contribute to the development of bioactive metallic implants.