Postadsorptive transitions in fibrinogen adsorbed to polyurethanes: changes in antibody binding and sodium dodecyl...

Residence time-dependent changes in fibrinogen after adsorption to six different polyurethanes were examined by measuring polyclonal antifibrinogen binding to the adsorbed protein. The amount of adsorbed fibrinogen that could be eluted by sodium dodecyl sulfate (SDS) was also measured. Baboon fibrinogen was first adsorbed from dilute plasma to the polymers, which were then stored in either buffer or buffered albumin solution prior to testing. Subsequently, the amount of antifibrinogen bound by the adsorbed fibrinogen was measured using a direct enzyme linked immunosorbent assay (ELISA). Alternatively, the surface with the adsorbed fibrinogen was soaked in a 3% SDS solution, and the amount of retained 125I-radiolabeled fibrinogen was measured. With increasing residence time, decreases in both antibody binding and the SDS elutability of the adsorbed fibrinogen occurred, but the rate of change was dependent on the polyurethane to which the fibrinogen was adsorbed. In addition, the antibody binding per unit of adsorbed fibrinogen, when measured immediately after the adsorption step, varied by approximately a factor of 3 among the various polyurethanes. When the protein-coated surfaces were stored in buffered albumin solution rather than buffer, the decrease in the reactivity of fibrinogen with residence time did not occur on some of the surfaces. This study shows that the chemical properties of the adsorbing surface influence the rate at which adsorbed fibrinogen undergoes change. The significance of the polymer-dependent changes in adsorbed fibrinogen with respect to blood reactions with polymers is discussed.