Although chemists rightfully argue that enzymes are “not different, just better” than synthetic catalysts, artificial enzymes created on purely synthetic or semi-natural platforms generally do not match their natural counterparts in performance. The deficiency of artificial enzymes has many reasons but a main roadblock is the lack of suitable synthetic strategies to construct multifunctional active sites with accurately positioned binding and catalytic groups. We present methods to convert dynamic micelles into cross-linked polymeric nanoparticles with well-defined binding sites through molecular imprinting. The nanoconfinement of the polymerization and cross-linking yield an extraordinary templating effect, with the imprint/nonimprint ratio in binding frequently reaching hundreds and sometimes 10,000. Installation of catalytic groups through postmodification turns the water-soluble nanoparticles into enzyme-like catalysts, with biomimetic or unnatural catalytic motifs. Our synthetic cellulases outperform some natural enzymes in cellobiose hydrolysis, with a kcat/kuncat value up to 1010. Our synthetic esterase could hydrolyze nonactivated alkyl esters at room temperature and neutral pH, while more reactive aryl esters stay intact in the same solution. As robust cross-linked polymeric nanoparticles, these “artificial enzymes” can function under conditions totally impossible for biocatalysts and can be converted into recyclable heterogenous catalysts when clicked onto a solid support.

Polymeric nanoparticle catalysts with enzyme-like catalytic efficiency and selectivity for glycan and ester hydrolysis

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ACS Spring 2023

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