Abstract

This chapter presents a study in which the adsorption of a model protein bovine serum albumin (BSA) on a 316L stainless steel surface, is examined by XPS (X-ray Photoelectron Spectroscopy) to determine the influence of Na+, Mg2+, and Ca2+ in solution on the interaction of proteins with the stainless steel surface, and to investigate the possible effect of adsorbed protein on the stainless steel surface composition. The XPS analysis of stainless steel samples immersed in saline solutions containing proteins (BSA) shows that the BSA is adsorbed on the stainless steel surface and that there is an effect of the salt on the protein adsorption. The data shows that the divalent cations (Ca2+ and Mg2+) enhance the BSA adsorption, whereas monovalent cations (Na+) have no effect on the BSA adsorption. The C1s and N1s XPS spectra are characteristic of the BSA, and thus it is concluded that the BSA remains chemically intact after adsorption on stainless steel. The stainless steel surface composition is analyzed after exposure to the aqueous solution of BSA with the different salts. In all cases the enrichment of Mo and Ni under the oxide layer as well as the enrichment of Cr3+ and Mo oxides in the oxide layer are observed, which shows that the adsorption of the protein does not modify the composition of the passive film.

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