An electrochemical biosensor for T4 polynucleotide kinase activity identification according to host-guest recognition among phosphate pillar[5]arene@palladium nanoparticles@reduced graphene oxide nanocomposite and toluidine blue.
Electrochemical biosensors
Gold electrode modification
Host–guest recognition
Palladium nanoparticles
Phosphate pillar[5]arene
T4 polynucleotide kinase
Toluidine blue
Journal
Mikrochimica acta
ISSN: 1436-5073
Titre abrégé: Mikrochim Acta
Pays: Austria
ID NLM: 7808782
Informations de publication
Date de publication:
16 09 2023
16 09 2023
Historique:
received:
11
06
2023
accepted:
02
09
2023
medline:
18
9
2023
pubmed:
16
9
2023
entrez:
15
9
2023
Statut:
epublish
Résumé
T4 polynucleotide kinase (T4 PNK) helps with DNA recombination and repair. In this work, a phosphate pillar[5]arene@palladium nanoparticles@reduced graphene oxide nanocomposite (PP5@PdNPs@rGO)-based electrochemical biosensor was created to identify T4 PNK activities. The PP5 used to complex toluidine blue (TB) guest molecules is water-soluble. With T4 PNK and ATP, the substrate DNA, which included a 5'-hydroxyl group, initially self-assembled over the gold electrode surface by chemical adsorption of the thiol units. Strong phosphate-Zr
Identifiants
pubmed: 37715009
doi: 10.1007/s00604-023-05983-w
pii: 10.1007/s00604-023-05983-w
doi:
Substances chimiques
graphene oxide
0
palladium oxide
B30901Q32J
Palladium
5TWQ1V240M
Phosphates
0
pillar(5)arene
0
Polynucleotide 5'-Hydroxyl-Kinase
EC 2.7.1.78
Tolonium Chloride
15XUH0X66N
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
394Subventions
Organisme : National Natural Science Foundation of China
ID : 21665027
Organisme : National Natural Science Foundation of China
ID : 21565031
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.
Références
Wang LK, Lima CD, Shuman S (2002) Structure and mechanism of T4 polynucleotide kinase: an RNA repair enzyme. EMBO J 21(14):3873–3880. https://doi.org/10.1093/emboj/cdf397
doi: 10.1093/emboj/cdf397
pubmed: 12110598
pmcid: 126130
Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JNM (2005) The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase. Mol Cell 17(5):657–670. https://doi.org/10.1016/j.molcel.2005.02.012
doi: 10.1016/j.molcel.2005.02.012
pubmed: 15749016
Tahbaz N, Subedi S, Weinfeld M (2012) Role of polynucleotide kinase/phosphatase in mitochondrial DNA repair. Nucleic Acids Res 40(8):3484–3495. https://doi.org/10.1093/nar/gkr1245
doi: 10.1093/nar/gkr1245
pubmed: 22210862
Sallmyr A, Rashid I, Bhandari SK, Naila T, Tomkinson AE (2020) Human DNA ligases in replication and repair. DNA Repair 93:102908. https://doi.org/10.1016/j.dnarep.2020.102908
doi: 10.1016/j.dnarep.2020.102908
pmcid: 8727047
Dumitrache LC, McKinnon PJ (2017) Polynucleotide kinase-phosphatase (PNKP) mutations and neurologic disease. Mech Ageing Dev 161:121–129. https://doi.org/10.1016/j.mad.2016.04.009
doi: 10.1016/j.mad.2016.04.009
pubmed: 27125728
Chatterjee A, Saha S, Chakraborty A, Silva-Fernandes A, Mandal SM, Neves-Carvalho A, Liu Y, Pandita RK, Hegde ML, Hegde PM, Boldogh I, Ashizawa T, Koeppen AH, Pandita TK, Maciel P, Sarkar PS, Hazra TK (2015) The role of the mammalian DNA end-processing enzyme polynucleotide kinase 3’-phosphatase in spinocerebellar Ataxia type 3 pathogenesis. PLOS Genet 11(1):e1004749. https://doi.org/10.1371/journal.pgen.1004749
doi: 10.1371/journal.pgen.1004749
pubmed: 25633985
pmcid: 4310589
Yannone SM, Roy S, Chan DW, Murphy MB, Huang S, Campisi J, Chen DJ (2001) Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase. J Biol Chem 276(41):38242–38248. https://doi.org/10.1074/jbc.m101913200
doi: 10.1074/jbc.m101913200
pubmed: 11477099
Shen J, Gilmore EC, Marshall CA, Haddadin M, Reynolds JJ, Eyaid W, Bodell A, Barry B, Gleason D, Allen K, Ganesh VS, Chang BS, Grix A, Hill RS, Topcu M, Caldecott KW, Barkovich AJ, Walsh CA (2010) Mutations in PNKP cause microcephaly, seizures and defects in DNA repair. Nat Genet 42:245–249. https://doi.org/10.1038/ng.526
doi: 10.1038/ng.526
pubmed: 20118933
pmcid: 2835984
Kalasova I, Hailstone R, Bublitz J, Bogantes J, Hofmann W, Leal A, Hanzlikova H, Caldecott KW (2020) Pathological mutations in PNKP trigger defects in DNA single-strand break repair but not DNA double-strand break repair. Nucleic Acids Res 48(12):6672–6684. https://doi.org/10.1093/nar/gkaa489
doi: 10.1093/nar/gkaa489
pubmed: 32504494
pmcid: 7337934
Freschauf GK, Karimi-Busheri F, Ulaczyk-Lesanko A, Mereniuk TR, Ahrens A, Koshy JM, Rasouli-Nia A, Pasarj P, Holmes CF, Rininsland F, Hall DG, Weinfeld M (2009) Identification of a small molecule inhibitor of the human DNA repair enzyme polynucleotide kinase/phosphatase. Cancer Res 69(19):7739–7746. https://doi.org/10.1158/0008-5472.can-09-1805
doi: 10.1158/0008-5472.can-09-1805
pubmed: 19773431
Mereniuk TR, Maranchuk RA, Schindler A, Penner-Chea J, Freschauf GK, Hegazy S, Lai R, Foley E, Weinfeld M (2012) Genetic screening for synthetic lethal partners of polynucleotide kinase/phosphatase: potential for targeting SHP-1-Depleted cancers. Cancer Res 72(22):5934–5944. https://doi.org/10.1158/0008-5472.can-12-0939
doi: 10.1158/0008-5472.can-12-0939
pubmed: 22962271
Mereniuk TR, El Gendy MAM, Mendes-Pereira AM, Lord CJ, Ghosh S, Foley E, Ashworth A, Weinfeld M (2013) Synthetic lethal targeting of PTEN-deficient cancer cells using selective disruption of polynucleotide kinase/phosphatase. Mol Cancer Ther 12(10):2135–2144. https://doi.org/10.1158/1535-7163.mct-12-1093
doi: 10.1158/1535-7163.mct-12-1093
pubmed: 23883586
pmcid: 3793902
Rasouli-Nia A, Karimi-Busheri F, Weinfeld M (2004) Stable down-regulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents. Proc Nat Acad Sci USA 101(18):6905–6910. https://doi.org/10.1073/pnas.0400099101
doi: 10.1073/pnas.0400099101
pubmed: 15100409
pmcid: 406440
Karimi-Busheri F, Rasouli-Nia A, Allalunis-Turner J, Weinfeld M (2007) Human polynucleotide kinase participates in repair of DNA double-strand breaks by nonhomologous end joining but not homologous recombination. Cancer Res 67(14):6619–6625. https://doi.org/10.1158/0008-5472.can-07-0480
doi: 10.1158/0008-5472.can-07-0480
pubmed: 17638872
Phillips DH, Arlt VM (2007) The
doi: 10.1038/nprot.2007.394
pubmed: 18007613
Wang LK, Shuman S (2001) Domain structure and mutational analysis of T4 polynucleotide kinase. J Biol Chem 276(29):26868–26874. https://doi.org/10.1074/jbc.m103663200
doi: 10.1074/jbc.m103663200
pubmed: 11335730
Chappell C, Hanakahi LA, Karimi-Busheri F, Weinfeld M, West SC (2002) Involvement of human polynucleotide kinase in double-strand break repair by non-homologous end joining. EMBO J 21:2827–2832. https://doi.org/10.1093/emboj/21.11.2827
doi: 10.1093/emboj/21.11.2827
pubmed: 12032095
pmcid: 126026
Whitehouse CJ, Taylor RM, Thistlethwaite A, Zhang H, Karimi-Busheri F, Lasko DD, Weinfeld M, Caldecott KW (2001) XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 104(1):107–117. https://doi.org/10.1016/s0092-8674(01)00195-7
doi: 10.1016/s0092-8674(01)00195-7
pubmed: 11163244
Liu HS, Ma CB, Wang J, Chen HC, Wang KM (2017) Label-free colorimetric assay for T4 polynucleotide kinase/phosphatase activity and its inhibitors based on G-quadruplex/hemin DNAzyme. Anal Biochem 517:18–21. https://doi.org/10.1016/j.ab.2016.10.022
doi: 10.1016/j.ab.2016.10.022
pubmed: 27984013
Lin L, Shi DM, Li QF, Wang GF, Zhang XJ (2016) Detection of T4 polynucleotide kinase based on a MnO
doi: 10.1039/c6ay00269b
Zhu J, Chen LT (2022) Highly efficient incorporation of dATP in terminal transferase polymerization forming the ploy (A)
doi: 10.1016/j.aca.2022.340080
pubmed: 35934340
Zhang YQ, Cai QQ, Yan XS, Jie GF (2023) Versatile fluorescence detection of T4 PNK and mRNA based on unique DNA nanomachine amplification. Anal Chim Acta 1251:341003. https://doi.org/10.1016/j.aca.2023.341003
doi: 10.1016/j.aca.2023.341003
pubmed: 36925292
Xie ZW, Wang XY, Chen SY, Zhao ZX, Zhao SH, Zhang WX, Luo LJ, Yi G (2022) Construction of a simple, localized and homogeneous fluorescence detection platform for T4 PNK activity based on tetrahedral DNA nanostructure-mediated primer exchange reaction. Microchem J 183:107989. https://doi.org/10.1016/j.microc.2022.107989
doi: 10.1016/j.microc.2022.107989
Qin YQ, Ke WK, Zhou YN, Zhu DD, Li YJ, Hu YG (2023) TtAgo sensor for the sensitive and rapid detection of T4 polynucleotide kinase activity. Sens Actuators B Chem 386:133753. https://doi.org/10.1016/j.snb.2023.133753
doi: 10.1016/j.snb.2023.133753
Chai YY, Cheng X, Xu GH, Wei FD, Bao J, Mei J, Ren DD, Hu Q, Cen Y (2020) A nanoplatform based on metal–organic frameworks and coupled exonuclease reaction for the fluorimetric determination of T4 polynucleotide kinase activity and inhibition. Microchim Acta 187:243. https://doi.org/10.1007/s00604-020-4194-y
doi: 10.1007/s00604-020-4194-y
Cao Y, Zhou Y, Lin YH, Zhu JJ (2021) Hierarchical metal−organic framework-confined CsPbBr 3 quantum dots and aminated carbon dots: a new self-sustaining suprastructure for electrochemiluminescence bioanalysis. Anal Chem 93:1818–1825. https://doi.org/10.1021/acs.analchem.0c04717
doi: 10.1021/acs.analchem.0c04717
pubmed: 33372764
Zhang GY, Chai HN, Tian MW, Zhu SF, Qu LJ, Zhang XJ (2020) Zirconium−metalloporphyrin frameworks−luminol competitive electrochemiluminescence for ratiometric detection of polynucleotide kinase activity. Anal Chem 92:7354–7362. https://doi.org/10.1021/acs.analchem.0c01262
doi: 10.1021/acs.analchem.0c01262
pubmed: 32319281
Yang JH, He GH, Wu WY, Deng WF, Tan YM, Xie QJ (2022) Sensitive photoelectrochemical determination of T4 polynucleotide kinase using AuNPs/SnS
doi: 10.1016/j.talanta.2022.123660
pubmed: 35689947
Li PP, Cao Y, Mao CJ, Jin BK, Zhu JJ (2019) TiO
doi: 10.1021/acs.analchem.8b04823
pubmed: 30562453
Tao JP, Liu ZQ, Zhu ZY, Zhang YL, Wang HB, Pang PF, Yang C, Yang WR (2022) Electrochemical detection of T4 polynucleotide kinase activity based on magnetic Fe
doi: 10.1016/j.talanta.2022.123272
pubmed: 35121542
Yan ZY, Shen XY, Zhou BL, Pan RY, Zhang B, Zhao CZ, Ren LH, Ming JJ (2021) Precise analysis of T4 polynucleotide kinase and inhibition by coupling personal glucose meter with split DNAzyme and ligation-triggered DNA walker. Sens Actuators B Chem 326:128831. https://doi.org/10.1016/j.snb.2020.128831
doi: 10.1016/j.snb.2020.128831
Mao JX, Chen X, Xu HH, Xu XQ (2020) DNAzyme-driven DNA walker biosensor for amplified electrochemical detection of T4 polynucleotide kinase activity and inhibition. J Electroanal Chem 874:114470. https://doi.org/10.1016/j.jelechem.2020.114470
doi: 10.1016/j.jelechem.2020.114470
Yan ZY, Deng PY, Liu Y (2019) Recent advances in protein kinase activity analysis based on nanomaterials. Int J Mol Sci 20(6):1440. https://doi.org/10.3390/ijms20061440
doi: 10.3390/ijms20061440
pubmed: 30901923
pmcid: 6471164
Song Z, Li Y, Teng H, Ding CF, Xu GY, Luo XL (2020) Designed zwitterionic peptide combined with sacrificial Fe-MOF for low fouling and highly sensitive electrochemical detection of T4 polynucleotide kinase. Sens Actuators B Chem 305:127329. https://doi.org/10.1016/j.snb.2019.127329
doi: 10.1016/j.snb.2019.127329
Li JL, Ma JH, Zhang YC, Zhang ZL, He GW (2019) A fluorometric method for determination of the activity of T4 polynucleotide kinase by using a DNA-templated silver nanocluster probe. Microchim Acta 186:48. https://doi.org/10.1007/s00604-018-3157-z
doi: 10.1007/s00604-018-3157-z
Zhang YL, Fang X, Zhu ZY, Lai YQ, Xu CL, Pang PF, Wang HB, Yang C, Barrow CJ, Yang WR (2018) A sensitive electrochemical assay for T4 polynucleotide kinase activity based on titanium dioxide nanotubes and a rolling circle amplification strategy. RSC Adv 8(67):38436–38444. https://doi.org/10.1039/c8ra07745b
doi: 10.1039/c8ra07745b
pubmed: 35559107
pmcid: 9090566
Song WL, Yin WS, Zhang ZH, He P, Yang XY, Zhang XR (2019) A DNA functionalized porphyrinic metal-organic framework as a peroxidase mimicking catalyst for amperometric determination of the activity of T4 polynucleotide kinase. Microchim Acta 186:149. https://doi.org/10.1007/s00604-019-3269-0
doi: 10.1007/s00604-019-3269-0
Lin MH, Wan H, Zhang J, Wang Q, Hu XY, Xia F (2020) Electrochemical DNA sensors based on MoS
doi: 10.1021/acsami.0c13385
pubmed: 32877162
Zhou YL, Yin HS, Zhao WW, Ai SY (2020) Electrochemical, electrochemiluminescent and photoelectrochemical bioanalysis of epigenetic modifiers: a comprehensive review. Coordin Chem Rev 424:213519. https://doi.org/10.1016/j.ccr.2020.213519
doi: 10.1016/j.ccr.2020.213519
Ma XH, Hao YQ, Dong XX, Xia N (2023) Biosensors with metal ion–phosphate chelation interaction for molecular recognition. Molecules 28(11):4394. https://doi.org/10.3390/molecules28114394
doi: 10.3390/molecules28114394
pubmed: 37298870
pmcid: 10254840
Liao Y, Zhang YQ, Su AW, Zhang YL, Wang HB, Yang WR, Pang PF (2023) Zr
doi: 10.1016/j.talanta.2023.124612
pubmed: 37141826
Hu Q, Kong JM, Han DX, Bao Y, Zhang XJ, Zhang YW, Niu L (2020) Ultrasensitive peptide-based electrochemical detection of protein kinase activity amplified by RAFT polymerization. Talanta 206:120173. https://doi.org/10.1016/j.talanta.2019.120173
doi: 10.1016/j.talanta.2019.120173
pubmed: 31514862
Ohtani S, Kato K, Fa S, Ogoshi T (2022) Host–guest chemistry based on solid-state pillar[n]arenes. Coord Chem Rev 462:214503. https://doi.org/10.1016/j.ccr.2022.214503
doi: 10.1016/j.ccr.2022.214503
Sathiyajith C, Shaikh RR, Han Q, Zhang Y, Meguellati K, Yang YW (2017) Biological and related applications of pillar[n]arenes. Chem Commun 53:677–696. https://doi.org/10.1039/c6cc08967d
doi: 10.1039/c6cc08967d
Yang K, Pei YX, Wen J, Pei ZC (2016) Recent advances in pillar[n]arenes: synthesis and applications based on host-guest interactions. Chem Commun 52:9316–9326. https://doi.org/10.1039/c6cc03641d
doi: 10.1039/c6cc03641d
Shamagsumova RV, Shurpik DN, Kuzin YI, Stoikov II, Rogov AM, Evtugyn GA (2022) Pillar[6]arene: electrochemistry and application in electrochemical (bio)sensors. J Electroanal Chem 913:116281. https://doi.org/10.1016/j.jelechem.2022.116281
doi: 10.1016/j.jelechem.2022.116281
Cao S, Zhou L, Liu C, Zhang HC, Zhao YX, Zhao YL (2021) Pillararene-based self-assemblies for electrochemical biosensors. Biosens Bioelectron 181:113164. https://doi.org/10.1016/j.bios.2021.113164
doi: 10.1016/j.bios.2021.113164
pubmed: 33744670
Evtyugin GA, Shurpik DN, Stoikov II (2020) Electrochemical sensors and biosensors on the pillar[5]arene platform. Russ Chem Bull Int Ed 69:859–874. https://doi.org/10.1007/s11172-020-2843-2
doi: 10.1007/s11172-020-2843-2
Wang J, Zhou L, Bei JL, Zhao QY, Li X, He JQ, Cai Y, Chen TT, Du YK, Yao Y (2022) An enhanced photo-electrochemical sensor constructed from pillar [5]arene functionalized Au NPs for ultrasensitive detection of caffeic acid. Talanta 243:123322. https://doi.org/10.1016/j.talanta.2022.123322
doi: 10.1016/j.talanta.2022.123322
pubmed: 35228106
Wang J, Bei JL, Guo X, Ding Y, Chen TT, Lu B, Wang Y, Du YK, Yao Y (2022) Ultrasensitive photoelectrochemical immunosensor for carcinoembryonic antigen detection based on pillar[5]arene-functionalized Au nanoparticles and hollow PANI hybrid BiOBr heterojunction. Biosens Bioelectron 208:114220. https://doi.org/10.1016/j.bios.2022.114220
doi: 10.1016/j.bios.2022.114220
pubmed: 35358775
Liang H, Zhao YT, Ye HZ, Li CP (2019) Ultrasensitive and ultrawide range electrochemical determination of bisphenol A based on PtPd bimetallic nanoparticles and cationic pillar[5]arene decorated graphene. J Electroanal Chem 855:113487. https://doi.org/10.1016/j.jelechem.2019.113487
doi: 10.1016/j.jelechem.2019.113487
Tan XP, He SH, Liu X, Zhao GF, Huang T, Yang L (2019) Ultrasensitive electrochemical sensing of dopamine by using dihydroxylatopillar[5]arene-modified gold nanoparticles and anionic pillar[5]arene-functionalized graphitic carbon nitride. Microchim Acta 186:703. https://doi.org/10.1007/s00604-019-3869-8
doi: 10.1007/s00604-019-3869-8
Hu X, Liu X, Zhang W, Qin S, Yao C, Li Y, Cao D, Peng L, Wang L (2016) Controllable construction of biocompatible supramolecular micelles and vesicles by water-soluble phosphate pillar[5,6]arenes for selective anti-cancer drug delivery. Chem Mater 28:3778–3788. https://doi.org/10.1021/acs.chemmater.6b00691
doi: 10.1021/acs.chemmater.6b00691
Luo D, Liu ZQ, Su AW, Zhang YL, Wang HB, Yang LJ, Yang WR, Pang PF (2024) An electrochemical biosensor for detection of T4 polynucleotide kinase activity based on host-guest recognition between phosphate pillar[5]arene and methylene blue. Talanta 266:124956. https://doi.org/10.1016/j.talanta.2023.124956
doi: 10.1016/j.talanta.2023.124956
pubmed: 37499362
Qian XC, Tan S, Li Z, Qu Q, Li L, Yang L (2020) A robust host-guest interaction controlled probe immobilization strategy for the ultrasensitive detection of HBV DNA using hollow HP5-Au/CoS nanobox as biosensing platform. Biosens Bioelectron 153:112051. https://doi.org/10.1016/j.bios.2020.112051
doi: 10.1016/j.bios.2020.112051
pubmed: 32056664
Yang L, Zhao H, Li YC, Ran X, Deng GG, Zhang YQ, Ye HZ, Zhao GF, Li CP (2016) Indicator displacement assay for cholesterol electrochemical sensing using a calix[6]arene functionalized graphene-modified electrode. Analyst 141:270–278. https://doi.org/10.1039/c5an01843a
doi: 10.1039/c5an01843a
pubmed: 26626104
Zhao H, Yan Y, Chen MJ, Hu TT, Wu KF, Liu HS, Ma CB (2019) Exonuclease III-assisted signal amplification strategy for sensitive fluorescence detection of polynucleotide kinase based on poly(thymine)-templated copper nanoparticles. Analyst 144:6689–6697. https://doi.org/10.1039/c9an01659g
doi: 10.1039/c9an01659g
pubmed: 31598619