Evidence map›Paper›PMID 41287267›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025

Synthetic Mimics of Serine Proteases via Covalent Imprinting of Photo-Protected Template Molecules for Aryl Amide Hydrolysis.

Rasmita Barik, Yan Zhao

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Rasmita BarikDepartment of Chemistry, Iowa State University, Ames, Iowa, USA.
Yan ZhaoDepartment of Chemistry, Iowa State University, Ames, Iowa, USA.ORCID https://orcid.org/0000-0003-1215-2565

Funding

Division of Chemistry CHE-2246635
6 · The paper itself

Abstract

The rational design of enzyme-mimicking catalysts remains in its early stages. Beyond the controversies surrounding the origin of the catalytic efficiency found in enzyme catalysis, a large challenge lies in the synthetic construction of multifunctional active sites with precisely positioned binding and catalytic groups. Here, we present a rational strategy to create serine protease-mimicking molecularly imprinted nanoparticles (MINPs) via covalent imprinting within cross-linkable micelles, followed by photo-deprotection of the polymerized template molecules. Unlike previously reported protease mimics that work on activated ester substrates, the MINP-based catalysts are able to hydrolyze aryl amides under mild conditions. In addition, substrate selectivity can be finely tuned through the modular design of the template molecules.

Indexed as

AmidesMolecular ImprintingNanoparticlesSerine ProteasesCatalysisHydrolysisMicellesAmidesMicellesSerine Proteasesartificial enzymehydrolysismicellemolecular imprintingphoto deprotection

Identifiers

PMID41287267
PMCPMC12731520

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.