Fibrinogen adsorption to receptor-like biomaterials made by pre-adsorbing peptides to polystyrene substrates

Two peptides from the ligand-binding site of the platelet receptor GPIIb/IIIa, residues 296-306 of GPIIb, designated B12 by D'Souza et al. (1991), and 300-311 of GPIIb, designated G13 by Taylor et al., (1992), as well as two control peptides, designated C14 and C20, were adsorbed to treated polystyrene substrates. Fibrinogen adsorption to the peptide-coated substrates was characterized. The specificity of I-125 labeled fibrinogen binding to the peptide-coated substrates was investigated by measuring the amount of fibrinogen adsorbed to each substrate and the inhibition of fibrinogen binding by RGDS peptide, bovine serum albumin, a divalent ion chelator (ethylene diamine tetra-acetic acid disodium salt), unlabeled fibrinogen and the B12 peptide. The results show that non-specific binding of fibrinogen to the B12-coated substrate is predominant under most conditions. Binding of monoclonal antibodies to fibrinogen adsorbed to the peptide coated substrates was characterized. The failure of several antibodies to bind fibrinogen adsorbed to the B12 substrate suggested that adsorption of fibrinogen to the B12-coated substrate alters its conformation relative to fibrinogen adsorbed to the bare substrate.