Human erythrocyte adhesion and spreading on protein-coated polymer surfaces

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Abstract
Protein adsorption is the first event which occurs when polymer surfaces are exposed to blood. The adsorption of proteins modifies the surface properties of the substrates and therefore influences subsequent cell—surface interactions. In an attempt to elucidate the fundamental mechanisms governing cell—proteinated‐surface interactions, the extent of fresh human erythrocyte adhesion and spreading on protein‐coated surfaces was examined. Five human serum proteins (albumin, fibrinogen, immunoglobulin G, fibronectin, and transferrin) were used at bulk concentrations ranging from 0.01 mg/mL to 50 mg/mL. Polymer substrates covering a wide range of wettability were employed. Protein adsorption significantly reduces erythrocyte adhesion and spreading on all test surfaces with minimum adhesion observed on fibrinogen: IgG > albumin > fibronectin > transferrin > fibrinogen. The extent of these effects is dependent on the nature of the adsorbed protein, the protein bulk concentration, and the surface properties of the underlying polymer substrates.

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