A combined surface activation and "grafting to" strategy was developed to convert divinylbenzene particles into weak cation exchangers suitable for protein separation. The initial activation step was based on plasma modification with bromoform, which rendered the particles amenable to further reaction with nucleophiles by introducing Br to a surface content of 11.2 atom-%, as determined by X-ray photoelectron spectroscopy. Grafting of thiol-terminated glydicyl methacrylate telomers to freshly plasma activated surfaces was accomplished without the use of added initiator, and the grafting was verified both by reduction in bromine content and the appearance of sulfur-carbon linkages, showing that the surface grafts were covalently bonded. Following grafting the attached glydicyl methacrylate telomer tentacles were further modified by a two-step procedure involving hydrolysis to 2,3-hydroxypropyl groups and conversion of hydroxyl groups to carboxylate functionality by succinic anhydride. The final material was capable of baseline separating four model proteins in 3 min by gradient cation exchange chromatography in a fully aqueous eluent.