Adsorption studies of human serum albumin, human γ-globulins, and human fibrinogen on the surface of P(S/PGL) microspheres

Adsorption of human serum albumin (HSA), human gamma-globulins (gammaG), and human fibrinogen (Fb) onto the surface of poly(styrene/alpha-t-butoxy-omega-vinylbenzyl-polyglycidol) microspheres (P(S/PGL)) with controlled fraction of polyglycidol in the interfacial layer was investigated. The microspheres were synthesized by the emulsifier-free radical copolymerization of styrene and alpha-t-butoxy-omega-vinylbenzyl-polyglycidol macromonomer (PGL). Macromonomers with number average molecular weights (M) over bar (n) = 950 and 2700 were used in the syntheses. Fraction of polyglycidol in the microsphere surface layer was varied from 0.22 to 0.44, depending on the composition of the monomer feed. It was found that the maximal surface concentration of adsorbed proteins and the equilibrium constant of protein adsorption decreased with increased fraction of polyglycidol in the microsphere surface layer. For microspheres with the highest fraction of polyglycidol at the surface the maximal surface protein concentration was c. ten times lower and the adsorption equilibrium constant was c. one hundred times lower than for the reference polystyrene microspheres. The dependence of maximal surface concentration of adsorbed proteins on the fraction of polyglycidol in the particle interfacial layer indicated random distribution of polyglycidol chains without formation of polyglycidol and polystyrene patches at the microspheres surface.