ABSTRACTIn the present work, the adsorption of albumin and fibrinogen on Ta, Nb, Ti and Zr oxidesthin films deposited on Si (100) wafers by magnetron sputtering was studied in order to get a better understanding of the correlation among the surface properties of these oxides and the protein adsorption phenomena on their surfaces. The surface energy, hydrophobicity, chemical composition, roughness and atomic order of the films were characterized. The films were immersedfor 45 minutes in single protein solutions; either albumin or fibrinogenand the adsorbed protein layer on the films was studied ex-situ in a dry ambient using bothX-ray photoelectron spectroscopy and atomic force microscopy.The adsorption of albumin and fibrinogen on the films modified the surface morphology and decreased the surface roughness for all the four different metal oxides. The XPS results confirmed the presence of the protein on the surface of the films and showed that the two proteins studied were adsorbed without undergoing a major chemical decomposition. A correlation between the surface roughness,the polar component of the surface energy of the films and the atomic percentage of nitrogen on the films after protein adsorption, an indirect signal of the amount of protein adsorbed, was found for albumin and fibrinogen adsorption on Ta, Nb and Ti oxides; the largest the roughness or the polar component the largest amount of adsorbed protein.
Probing Protein Aggregation at Buried Interfaces: Distinguishing Adsorbed Protein Monomer, Dimer, and Monomer-Dimer Mixture in Situ
