Characterization of proteins and fibroblasts on thin inorganic films.

The ability of biomaterial surfaces to regulate cell behavior requires control over surface chemistry and material microstructure. One of the goals in the development of silicon-based biomedical devices such as biosensors or drug delivery systems is improved biocompatibility which may be achieved through the deposition or adsorption of thin films. In this study, films of single crystal silicon, stoichiometric and low stress silicon nitride, doped and undoped polysilicon, as well as Arg-Gly-Asp (RGD) peptide adsorbed surfaces characterized in terms of protein adsorption or cellular adhesion for a period of four days. Protein adsorption studies using fibrinogen and albumin, two proteins implicated in cellular adhesion and surface activity, reveal that low stress silicon nitride surfaces have a 223%+/-2.50% greater protein adsorption compared to undoped polysilicon surfaces, followed by silicon nitride, unmodified silicon, and doped polysilicon surfaces, respectively. The thickness of the adsorbed albumin and fibrinogen layer on various thin films was measured by ellipsometry and compared to contact angle measurements. The greatest cellular adhesion was observed on undoped polysilicon, followed by unmodified (control) silicon, low stress silicon nitride, silicon nitride, and doped polysilicon surfaces. Cellular binding supports the differential protein adsorption found on modified and unmodified silicon surfaces. Understanding the biological response to thin films will allow us to design more appropriate interfaces for implantable diagnostic and therapeutic silicon-based microdevices.