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

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 mech...

Full description

Saved in:
Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: MDPI AG 2025-01-01
Series:Biosensors
Subjects:
Online Access:https://www.mdpi.com/2079-6374/15/1/12
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1832588896345522176
author 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
author_facet 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
author_sort Raphael I. Adeoye
collection DOAJ
description 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.
format Article
id doaj-art-392bd71b596b4578a633620a14c65f1b
institution Kabale University
issn 2079-6374
language English
publishDate 2025-01-01
publisher MDPI AG
record_format Article
series Biosensors
spelling doaj-art-392bd71b596b4578a633620a14c65f1b2025-01-24T13:25:25ZengMDPI AGBiosensors2079-63742025-01-011511210.3390/bios15010012Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymesRaphael I. Adeoye0Theresia K. Ralebitso-Senior1Amanda Boddis2Amanda J. Reid3Francesca Giuntini4Amos A. Fatokun5Andrew K. Powell6Adaoha Ihekwaba-Ndibe7Sylvia O. Malomo8Femi J. Olorunniji9School of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKSchool of Life Sciences, Coventry University, Coventry CV1 2DS, UKDepartment of Biochemistry, University of Ilorin, Ilorin 240003, Kwara State, NigeriaSchool of Pharmacy & Biomolecular Sciences, Faculty of Health, Innovation, Technology and Science, Liverpool John Moores University, Liverpool L3 3AF, UKG-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.https://www.mdpi.com/2079-6374/15/1/12G-quadruplexDNAzymessperminemultivalent G-quartetsbiosensingnanozymes
spellingShingle 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
Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes
Biosensors
G-quadruplex
DNAzymes
spermine
multivalent G-quartets
biosensing
nanozymes
title Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes
title_full Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes
title_fullStr Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes
title_full_unstemmed Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes
title_short Spermine Enhances the Peroxidase Activities of Multimeric Antiparallel G-quadruplex DNAzymes
title_sort spermine enhances the peroxidase activities of multimeric antiparallel g quadruplex dnazymes
topic G-quadruplex
DNAzymes
spermine
multivalent G-quartets
biosensing
nanozymes
url https://www.mdpi.com/2079-6374/15/1/12
work_keys_str_mv AT raphaeliadeoye spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT theresiakralebitsosenior spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT amandaboddis spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT amandajreid spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT francescagiuntini spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT amosafatokun spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT andrewkpowell spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT adaohaihekwabandibe spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT sylviaomalomo spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes
AT femijolorunniji spermineenhancestheperoxidaseactivitiesofmultimericantiparallelgquadruplexdnazymes