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Abstract: Enzymes have substrate-tailored active sites with optimized molecular recognition and catalytic features. Although many different platforms have been used by chemists to construct enzyme mimics, it is challenging to tune the structure of their active sites systematically. By molecularly imprinting template molecules within doubly cross-linked micelles, we created protein-sized nanoparticles with catalytically functionalized binding sites. These enzyme mimics accelerated the hydrolysis of activated esters thousands of times over the background reaction, whereas the analogous catalytic group (a nucleophilic pyridyl derivative) was completely inactive in bulk solution under the same conditions. The template molecules directly controlled the size and shape of the active site and modulated the resulting catalyst's performance at different pHs. The synthetic catalysts displayed Michaelis-Menten enzymatic behavior and, interestingly, reversed the intrinsic reactivity of the activated esters during the hydrolysis
Template and target information: trasition state analogue, TSA
Author keywords: Micelle, nanoparticles, catalysis, molecular imprinting, hydrolysis