Evidence map›Paper›PMID 39852063›Full record

ArticleBiosensors2025

Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes.

Raphael I Adeoye, Theresia K Ralebitso-Senior, Amanda Boddis, Amanda J Reid, Francesca Giuntini, Amos A Fatokun, Andrew K Powell, Adaoha Ihekwaba-Ndibe, Sylvia O Malomo, Femi J Olorunniji

Abstract read
In one paragraph

Article in Biosensors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

10 authors.

Raphael I AdeoyeSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.ORCID 0000-0003-3367-4901
Theresia K Ralebitso-SeniorSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.ORCID 0000-0002-2404-0993
Amanda BoddisSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.
Amanda J ReidSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.
Francesca GiuntiniSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.ORCID 0000-0002-3444-8183
Amos A FatokunSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.ORCID 0000-0001-5183-7589
Andrew K PowellSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.
Adaoha Ihekwaba-NdibeSchool of Life Sciences, Coventry University, Coventry CV1 2DS, UK.
Sylvia O MalomoDepartment of Biochemistry, University of Ilorin, Ilorin 240003, Kwara State, Nigeria.ORCID 0000-0002-7575-6086
Femi J OlorunnijiSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UK.ORCID 0000-0001-9389-2981

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-quadruplex (G4) DNAzymes with peroxidase activities hold potential for applications in biosensing. While these nanozymes are easy to assemble, they are not as efficient as natural peroxidase enzymes. Several approaches are being used to better understand the structural basis of their reaction mechanisms, with a view to designing constructs with improved catalytic activities. Spermine alters the structures and enhances the activities of some G4 DNAzymes. The reported effect of spermine in shifting the conformation of some G4 DNAzymes from antiparallel to parallel has not been tested on multimeric G4 DNAzymes. In this study, we examined the effects of spermine on the catalytic activities of multivalent constructs of Bcl2, c-MYC, PS2.M, and PS5.M. Our findings show that spermine significantly improved the peroxidase activity of PS2.M, an antiparallel G4 DNAzyme, while there was no significant effect on c-MYC, which already exists in a parallel conformation. The addition of spermine led to a substantial increase in the initial velocity of PS2.M and its multimeric form, enhancing it by approximately twofold. Therefore, spermine enhancement offers promise in expanding the range of DNAzymes available for use as biosensing tools.

Indexed as

Biosensing TechniquesDNA, CatalyticG-QuadruplexesPeroxidasePeroxidasesSpermineDNA, CatalyticPeroxidasePeroxidasesSperminebiosensingDNAzymesG-quadruplexmultivalent G-quartetsnanozymesspermine

Identifiers

PMID39852063
PMCPMC11763995

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Registered trials

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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.