The interaction of macromolecular solutions with macromolecular monolayers adsorbed on a hydrophobic surface.

In order to elucidate the general patterns of intermacromolecular surface interactions that may be involved in hemocompatibility phenomena, monolayers of representative macromolecules on an octadecylsilylated glass surface were exposed to solutions of other macromolecules, and the changes in interfacial composition were characterized by zeta potential-pH titration curves, as measured by alternating flow streaming current analysis and, in some cases, by radiotracer labeling. Experiments with poly(vinylpyrrolidone) (PVP), a blood-compatible linear polymer; bovine serum albumin (BSA), a representative serum protein; whole human serum (HS), a complex mixture of proteins; and erythrocyte surface glycoprotein (GP), an extended-chain macromolecular amphiphile, showed the following: 1) Penetration of the original monolayer occurred within 24 hr in 9 of the 12 possible cases; it did not occur for BSA or HS monolayers exposed to PVP, and probably not for PVP exposed to GP. 2) In all cases, penetration was accompanied by no more than partial displacement of the original monolayer, thereby generating a mixed monolayer. Each of the six possible binary mixed monolayers could be obtained by at least one of the two possible mixing sequences. 3) In the three binary systems containing BSA, the formation of the mixed monolayer could be related to increased adsorption in the two-component system. 4) The two components of the mixed monolayers were not equally distributed across their thicknesses: thus, the outer surfaces of the PVP-BSA and (at neutral pH) the PVP-HS mixed monolayers contained only PVP; that of the BSA-HS mixtures only HS. In the PVP-HS, and probably the GP-BSA and GP-HS mixed monolayers, the composition of the outer surface appeared pH-dependent. The resultant zeta potential versus pH profiles in the latter two cases resembled those of intact blood cells. The results suggest that neither the compact monolayers of globular proteins nor the diffuse monolayers of randomly coiled water-soluble polymers can, by their prior adsorption on a synthetic surface, prevent the subsequent adsorption of other globular macromolecules. It is possible that the randomly coiled polymers may impede the adhesion of platelets to the substrate since the results indicate that the adsorption of such polymers causes a displacement of the shear plane.