Diamond and SiC both process extraordinary biocompatible, electronic, and chemical properties. A combination of diamond and SiC may lead to highly stable materials, e.g., for implants or biosensors with excellent sensing properties. Here we report on the controllable surface chemistry of diamond//beta-SiC composite films and its effect on protein adsorption. For systematic and high-throughput investigations, novel diamond/beta-SiC composite films with gradient composition have been synthesized using the hot filament chemical vapor deposition (HFCVD) technique. As revealed by scanning electron microscopy (SEM), the diamond/beta-SiC ratio of the composite films shows a continuous change from pure diamond to beta-SiC over a length of similar to 10 mm on the surface. Xray photoelectron spectroscopy (XPS) and time-of-flight secondary ion mass spectrometry (ToF-SIMS) was employed to unveil the surface termination of chemically oxidized and hydrogen treated surfaces. The surface chemistry of the composite films was found to depend on diamond/beta-SiC ratio and the surface treatment. As observed by confocal fluorescence microscopy, albumin and fibrinogen were preferentially adsorbed from buffer: after surface oxidation, the proteins preferred to adsorb on diamond rather than on beta-SiC, resulting in an increasing amount of proteins adsorbed to the gradient surfaces with increasing diamond/beta-SiC ratio. By contrast, for hydrogen-treated surfaces, the proteins preferentially adsorbed on beta-SiC, leading to a decreasing amount of albumin adsorbed on the gradient surfaces with increasing diamond/beta-SiC ratio. The mechanism of preferential protein adsorption is discussed by considering the hydrogen bonding of the water self-association network to OH-terminated surfaces and the change of the polar surface energy component, which was determined according to the van Oss method. These results suggest that the diamond/beta-SiC gradient film can be a promising material for biomedical applications which require good biocompatibility and selective adsorption of proteins and cells to direct cell migration.