Evidence map›Paper›PMID 36636357›Full record

ReviewiScience2023

Supramolecular enzyme-mimicking catalysts self-assembled from peptides.

Qing Liu, Akinori Kuzuya, Zhen-Gang Wang

Abstract readReview
In one paragraph

Review in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. Nanozymes Integrated Biochips Toward Smart Detection System.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026
    Review
  4. Article
  5. Review
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  8. Supramolecular Gels as Active Tools for Reaction Engineering.Angewandte Chemie (International ed. in English) · 2025
    Review
  9. Review
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  11. Article
  12. Article
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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

3 authors.

Qing LiuDepartment of Chemistry and Materials Engineering, Kansai University, Yamate-cho 3-3-35, Suita, Osaka 564-8680, Japan.
Akinori KuzuyaDepartment of Chemistry and Materials Engineering, Kansai University, Yamate-cho 3-3-35, Suita, Osaka 564-8680, Japan.
Zhen-Gang WangState Key Laboratory of Organic-Inorganic Composites, Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural enzymes catalyze biochemical transformations in superior catalytic efficiency and remarkable substrate specificity. The excellent catalytic repertoire of enzymes is attributed to the sophisticated chemical structures of their active sites, as a result of billions-of-years natural evolution. However, large-scale practical applications of natural enzymes are restricted due to their poor stability, difficulty in modification, and high costs of production. One viable solution is to fabricate supramolecular catalysts with enzyme-mimetic active sites. In this review, we introduce the principles and strategies of designing peptide-based artificial enzymes which display catalytic activities similar to those of natural enzymes, such as aldolases, laccases, peroxidases, and hydrolases (mainly the esterases and phosphatases). We also discuss some multifunctional enzyme-mimicking systems which are capable of catalyzing orthogonal or cascade reactions. We highlight the relationship between structures of enzyme-like active sites and the catalytic properties, as well as the significance of these studies from an evolutionary point of view.

Indexed as

BiomoleculesChemistryPeptidesSupramolecular chemistry

Identifiers

PMID36636357
PMCPMC9830222

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.