Functional coupling resins have been used to generate various protein- and ligand-immobilized gels for protein purification, proteomic research, drug development and synthetic biology. Recently, drug-immobilized resins have found broader applications for the analysis of drug-protein interactions, which are interfered with by the drug substances. Non-specific protein binding to the resin, not to the immobilized drug, is a common problem in the characterization of the bound proteins. Many commercial resins have more or less hydrophobic properties, leading to non-specific adsorption of proteins, in particular hydrophobic proteins. In addition, some resins are chemically unstable against the conditions used for drug immobilization: organic solvents are often used in immobilization reactions. We have developed a novel resin with functional amine group. It is a synthetic resin and hence chemically stable, and has a highly hydrophilic surface, minimizing non-specific protein adsorption. In addition, the resin surface can be made even more hydrophilic by surface coating. A couple of examples demonstrate its superior property for characterization of drug-protein interactions.
Keywords: Drug-protein interaction, affinity resin
