Abstract: Molecularly imprinted polymers (MIPs) are synthetic affinity matrices capable of selective binding a specific target molecule. A strategy for competitive selectivity studies is developed providing information on the selective binding properties of MIPs in complex matrices. Batch rebinding experiments entail the target protease, two other proteins, and MIP nanobeads. The protease is inhibited by addition of pepstatin thus quenching the degradation of the other proteins. The proteins are analyzed via sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The relevance of competitive selectivity studies for the evaluation of MIP performance is further emphasized by comparison to single protein rebinding experiments
Author keywords: competitive selectivity study, inhibition study, Molecularly imprinted polymer, protease, Protein-imprinted polymer