Evidence map›Paper›PMID 42003732›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Mechanozyme: An Artificial Enzyme With a Mechanophore Framework.

Jiahao Ji, Pravin Pokhrel, Sajan Shakya, Bishal Pokhrel, Grinsun Sharma, Pratiksha Chaudhary, Hao Shen, Hanbin Mao

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. 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

8 authors.

Jiahao JiDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.ORCID https://orcid.org/0000-0002-6189-7750
Pravin PokhrelDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.
Sajan ShakyaDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.
Bishal PokhrelDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.
Grinsun SharmaDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.
Pratiksha ChaudharyDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.
Hao ShenDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.
Hanbin MaoDepartment of Chemistry and Biochemistry, Kent State University, Kent, Ohio, USA.ORCID https://orcid.org/0000-0002-6720-9429

Funding

Supplemental Request for Mechanical Modulation of Cell Migrations by DNA NanoassembliesR01CA252827 · NCI · KENT STATE UNIVERSITY · PI Hanbin Mao · 2023 to 2026
$1.4M
National Science Foundation Che 2247709NCI NIH HHS R01 CA252827NIH HHS R01 CA252827
6 · The paper itself

Abstract

Conformational flexibility of natural enzymes, characterized by marginal stability, displays functional variations. In this work, we uncovered that artificial DNAzymes made of G-quadruplex (GQ)-hemin complexes also display this marginal stability phenomenon. Through single-molecule fluorescent MT-HILO (Magnetic Tweezers coupled with Highly Inclined and Laminated Optical sheet), we recorded the highest peroxidase activity among all known natural or artificial enzymes when the GQ mechanophore inside the DNAzymes was destabilized by an external force. We name enzymes with such force-responsive marginal stability "mechanozymes" to reflect the mechanical modulation of enzymatic activities. To set the stage for mechanical modulation on mechanozymes beyond the single-molecule level, ultrasonication was applied to enhance the catalytic function of a large ensemble of mechanozymes by weakening their GQ mechanophore structures. This work not only established marginal stability in artificial enzymes for the first time, but it also provided unprecedented mechanical modulation on catalytic activities, both of which are expected to have profound ramifications for catalysis exploited across the fields of chemistry and biosciences.

Indexed as

DNA, CatalyticG-QuadruplexesHeminDNA, CatalyticHeminDNAzymemarginal stabilitymechanical modulationmechanochemistryultrasonication

Identifiers

PMID42003732
PMCPMC13334946

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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.