Spectroscopic ellipsometry (SE) is a non-destructive technique, with high sensitivity, that can be applied both in air and in liquid ambient and perform very fast measurements. These advantages together with the use of advanced modeling procedures regarding SE data can provide valuable information for the study of biological samples. The aim of this work is to explore the protein adsorption phenomena and mechanisms of two basic blood plasma proteins on amorphous hydrogenated carbon (a-C:H) thin films, grown with rf reactive magnetron sputtering on c-Si substrates. The proteins Human Serum Albumin (HSA) and Fibrinogen (Fib), which play an important role in preventing and causing thrombi formation, respectively, were studied. Their adsorption was monitored in real-time (msec time) in Vis to UV spectral region for two pH values (at physiological conditions and at the protein’s isoelectric point) and on a-C:H thin films with different deposition conditions, in order to better comprehend protein adsorption and contribute to the improvement of potential biomaterials properties through controlling their growth conditions. Complementary AFM and Fourier Transform IR-SE measurements were made to provide additional information about surface nanotopography and bonding configuration of the a-C:H films, to describe in detail the bio/non-bio interactions. The a-C:H films deposition conditions as well as the pH of the protein solution affect protein adsorption rate. This is due to the surface nanostructural characteristics and bonding structure (in the case of different growth conditions of the a-C:H thin films) and due to the change of the protein molecules charge and the change of the lateral electrostatic interactions between them, for different pH of the protein solution.

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