ArticleACS catalysis2025
Turning Enzyme Models into Model Enzymes in a Substrate-Tailored, Desolvated Active Site.
Article in ACS catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Synthetic Mimics of Serine Proteases via Covalent Imprinting of Photo-Protected Template Molecules for Aryl Amide Hydrolysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Bifunctional Catalysis of Aldol Reactions by Foldamer Dihydrazides: Assessment of Conformational Preorganization.Journal of the American Chemical Society · 2025Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Once taken out of the active sites, the same functional groups used by enzymes for catalysis tend to lose their "magical" catalytic power in small-molecule enzyme models. We report a small-molecule enzyme model that activates a benzylic alcohol by a nearby amine for the nucleophilic attack of an activated ester. Only when the two groups are placed inside a substrate-tailored hydrophobic pocket can they display catalytic turnovers and even become reactive enough to hydrolyze amides catalytically near physiological conditions, a long-standing goal for synthetic protease mimics. These results suggest that the large gap between the innumerable catalytically incompetent small-molecule enzyme models made by chemists and true enzyme-like catalysts could be bridged by environmental engineering, which in this work enables a simple combination of a tertiary amine and an alcohol to replicate the catalytic properties of serine protease in hydrolyzing aryl amides with substrate specificity.
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Registered trials
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