Binding of proteins to copolymers of varying hydrophobicity.

Hydrophobic interactions between proteins and amphiphilic polyelectrolytes were studied by frontal analysis continuous capillary electrophoresis (Gao et al., Analytical Chemistry, 1997, Vol. 69, pp. 2945-2951). Binding isotherms were obtained for beta-lactoglobulin and for bovine serum albumin interacting with a series of alternating copolymers of maleic acid and alkyl-vinyl ethers of varying hydrophobicity. Although binding between proteins and copolymers increases with increasing alkyl chain length, a minimum alkyl chain length of 3-4 methylenes is required for significant hydrophobic interactions to occur. These copolymers, like other polyamphiphiles, can form intrapolymer micelles, and the extent of such micellization decreases with increasing degree of carboxylate ionization. Binding results obtained at different pHs suggest that competition exists between intrapolymer micelle formation and protein-polymer hydrophobic interactions.