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Phys. Chem. Chem. Phys., 2008, 10, 2502 - 2512, DOI: 10.1039/b719371h
Adsorption of fibrinogen on a biomedical-grade stainless steel 316LVM surface: a PM-IRRAS study of the adsorption thermodynamics, kinetics and secondary structure changes
Marie-Josee Desroches and Sasha Omanovic
Polarization-modulation infrared reflection–absorption spectroscopy (PM-IRRAS) was employed to investigate the interaction of serum protein fibrinogen with a biomedical-grade 316LVM stainless steel surface, in terms of the adsorption thermodynamics, kinetics and secondary structure changes of the protein. Apparent Gibbs energy of adsorption values indicated a highly spontaneous and strong adsorption of fibrinogen onto the surface. The kinetics of fibrinogen adsorption were successfully modeled using a pseudo first-order kinetic model. Deconvolution of the amide I bands indicated that the adsorption of fibrinogen on 316LVM results in significant changes in the protein
s secondary structure that occur predominantly within the first minute of adsorption. Among the investigated structures, the 
-helix structure undergoes the smallest changes, while the 
-sheet and -turns structures undergo significant changes. It was shown that lateral interactions between the adsorbed molecules do not play a role in controlling the secondary structure changes. An increase in temperature induced changes in the secondary structure of the protein, characterized by a loss of the -helical content and its transformation into the -turns structure.
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