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Binding of proteins to copolymers of varying hydrophobicity
Author(s) -
Gao Jeff Y.,
Dubin Paul L.
Publication year - 1999
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199902)49:2<185::aid-bip6>3.0.co;2-6
Subject(s) - chemistry , copolymer , micelle , amphiphile , polymer chemistry , alkyl , hydrophobic effect , polyelectrolyte , carboxylate , maleic acid , polymer , capillary electrophoresis , bovine serum albumin , organic chemistry , chromatography , aqueous solution
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 β‐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. © 1999 John Wiley & Sons, Inc. Biopoly 49: 185–193, 1999