Although a number of procedures to create synthetic polymer nanoparticles (NPs) with an intrinsic affinity to target biomacromolecules have been published, little has been reported on strategies to control the binding kinetics of target recognition. Here, we report an enzyme-mimic strategy to control binding/dissociation rate constants of NPs, which bind proteins through multipoint interactions, by taking advantage of the temperature-responsive coil-globule phase transition of poly-N-isopropylacrylamide (PNIPAm)-based NPs. PNIPAm NPs with a "flexible" random-coil conformation had a faster binding rate than NPs with a "rigid" globule conformation; however, the dissociation rate constant remained unchanged, resulting in stronger affinity. The dissociation rate of the "flexible" NPs was decelerated by the "induced-fit"-type conformation change of polymers around the coil-globule phase transition temperature, resulting in the formation of the most stable NP-protein complexes. These results provide a guide for designing plastic antibodies with tailor-made binding kinetics and equilibrium constants.