Ternary Protein Adsorption onto Brushes: Strong versus Weak

Abstract

Attractive interactions between proteins and polyethylene glycol (PEG) give rise to ternary adsorption within PEG brushes. Experimental evidence suggests two ternary adsorption modes: (i) weak, due to nonspecific weak attraction between PEG monomers and the surface of the protein, as exemplified by serum albumin and (ii) strong, due to strong binding of PEG segments to specific protein sites as it occurs for PEG antibodies, which can involve the terminal adsorption of free chain ends or backbone adsorption due to binding to interior chain segments. Ternary adsorption affects the capacity of brushes to repress protein adsorption. The strong adsorption of antibodies can trigger an immune response that may affect the biocompatibility of the surface. Theoretical adsorption isotherms and protein concentration profiles of the three cases are compared for "parabolic" brushes, allowing for the grafting density, 1/Sigma, and degree of polymerization of the PEG chains, N, as well as the volume and surface area of the proteins. The amount of adsorbed protein per unit area, Gamma, exhibits a mode-specific maximum in all three cases. For backbone and weak adsorption, Gamma approximately N, whereas for terminal adsorption, Gamma approximately N0. In every case, the concentration profile of adsorbed proteins, ctern(z), exhibits a maximum at zmax>0 that shifts outward as Sigma decreases; zmax=0 occurs only for weak and backbone adsorption at a high Sigma value.