Fibrinogen adsorption at heparinized silica interfaces : history dependence and protein concentration effects Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/gf06g507k

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  • Adipic dihydrazide-modified heparin was prepared and subsequently immobilized on surface-activated silica wafers. X-ray photoelectron spectroscopy (XPS) was used to quantify the elemental composition of the silica surface at each stage of activation and results showed that successful immobilization had taken place. Contact angle measurements were made to verify the high hydrophilicity of the heparinized and unheparinized silica surfaces. In situ ellipsometry was used to study protein concentration effects on adsorption kinetics exhibited by human plasma fibrinogen on unheparinized and heparinized silica. The adsorbed amount of fibrinogen increased with concentration, on each type of surface. At all concentrations, fibrinogen adsorbed in diminished amounts and at a slower rate on heparinized as compared to unheparinized silica. Buffer elution experiments showed that fibrinogen was less tightly bound on heparinized silica. To examine the history dependence of adsorption, fibrinogen was added for a second time, after rinsing. The difference in adsorption rates between the first and second adsorption cycle evaluated at identical mass density, indicated that post-adsorptive molecular rearrangements had taken place. These rearrangements presumably involved aggregation of adsorbed fibrinogen, in this way increasing unoccupied area at the interface. Fibrinogen was postulated to be more mobile on heparinized silica.
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