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A Bait‐and‐Switch Method for the Construction of Artificial Esterases for Substrate‐Selective Hydrolysis
Author(s) -
Hu Lan,
Zhao Yan
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201900560
Subject(s) - chemistry , catalysis , phosphonate , molecular imprinting , selectivity , combinatorial chemistry , micelle , template , active site , monomer , hydrolysis , imprinting (psychology) , substrate (aquarium) , molecule , organic chemistry , polymer , nanotechnology , materials science , aqueous solution , biochemistry , oceanography , geology , gene
Outcomes of chemical reactions are generally dominated by the intrinsic reactivities of reaction partners, but enzymes frequently override such constraints to transform less reactive molecules in the presence of more reactive ones. Despite the attractiveness of such catalysis, it is difficult to build synthetic catalysts with these features. Micellar imprinting is a powerful method to create template‐complementary binding sites inside protein‐sized water‐soluble nanoparticles. When a photocleavable functional monomer was used to bind two phosphonate/phosphate templates as transition‐state analogues, active sites with predetermined size and shape were formed inside doubly cross‐linked micelles through molecular imprinting. Postmodification replaced the binding group with a catalytic pyridyl group, forming highly selective artificial esterases. The catalysts displayed enzyme‐like kinetics and turnover numbers that were in the hundreds. The selectivity of the catalysts, derived from the substrate‐complementary imprinted active sites, enabled transformation of less reactive esters in the presence of more reactive ones.