Adsorption of proteins on spherical polyelectrolyte brushes in aqueous solution

We consider the adsorption of bovine serum albumin (BSA) on spherical polyelectrolyte brushes (SPB). The SPB consist of a solid polystyrene core of 100 nm diameter onto which linear polyelectrolyte chains [poly(acrylic acid), (PAA)] are grafted. The adsorption of BSA is studied at a pH of 6.1 at different concentrations of added salt and buffer. We observe strong adsorption of BSA onto the SPB despite the effect that the particles as well as the dissolved BSA are charged negatively. The adsorption of BSA is strongest at low salt concentration and decreases drastically with increasing amounts of added salt. Virtually no adsorption takes place at salt concentration of 0.1 M. Moreover, the adsorbed protein can be washed out again by raising the ionic strength from low to high values. A major driving force for the adsorption is located at a lower pH within the brush at low ionic strength. Thus, the isoelectric point of the protein may be approached or even reached. In this case strong interaction between the SPB and the protein results. Moreover, the negative charge of the polyelectrolyte interacts with the patches of positive charges on the protein. In this way the protein becomes a multivalent counterion within the brush and monovalent counterions will be released. All results demonstrate that the SPB present a new class of colloidal carrier particles whose interaction with proteins can be tuned in a well-defined fashion