Adsorption of proteins from plasma to a series of hydrophilic‐hydrophobic copolymers. II. Compositional analysis with the prelabeled protein technique

Abstract

Plasma protein adsorption is an important initial event in the response of tissue to foreign materials. Little is known about the way in which the chemical properties of materials influence the nature of the adsorbed layer and thus the later cellular responses. In this study, the amounts of fibrinogen, immunoglobulin G, albumin, and hemoglobin adsorbed from plasma to a series of HEMA-EMA random copolymers varying in hydrophilicity was measured. The adsorption of each protein varied in a characteristic way with copolymer composition probably reflecting a different affinity of the proteins for the various copolymers. A complex variation in the composition of the adsorbed protein layer on polymers varying in hydrophilicity was thus evident. Surface enrichment of the proteins, calculated as the ratio of the surface and bulk fraction of each protein, also varied with copolymer composition, and indicated substantial differences in the composition of the surface and bulk phases. Surface area variations among the copolymers, preferential adsorption of ¹²⁵I proteins, and the possibility of structural degradation of ¹²⁵I proteins in plasma were investigated but did not appear to influence the adsorption results. The ability of polymers to fractionate plasma proteins and concentrate them at their surface is concluded to be a key factor in the complex processes which determine the compatibility of polymers in vivo.