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Efficient AuPd@GO-based electrochemical nanoprobe for sensitive detection of histone acetylase activity and its inhibitor

  • Qiong Liu
  • Linfei Yang
  • Yuqi SheEmail author
  • Yufang HuEmail author
Research Paper
  • 18 Downloads

Abstract

Histone acetylase (HAT p300), which has aroused great concern in fundamental research and clinical applications, serves as one class of significant tumor markers. In our work, a sensitive electrochemical immunoassay for testing HAT p300 based on both graphene-assisted supported AuPd nanomaterial (AuPd@GO composite) and a typical amperometric i-t technique with fast response is developed favorably. The AuPd@GO-based sensing mechanisms are distributed as follows: the HAT p300 derived acetylation reaction occurs at the customized peptide-immobilized electrode; the AuPd@GO composite acts as carrier to immobilize acetyl antibody, thus constructing a sandwich-type electrochemical immunosensor via an antigen and antibody interaction; importantly, a distinct electrochemical signal could be caught due to the AuPd@GO nanomaterial with a favorable electrocatalytic property to the commercialized 3,3,5′,5′-tetramethyl benzidine solution (TMB). Taking advantage of AuPd@GO composite, the established immunosensor displays a wide linear range from 1 pM to 1000 nM, and the detection limit is 0.5 pM (S/N = 3) for HAT p300. Next, the biosensor is also used to analyze the inhibitor of HAT p300 successfully, which is promising for promoting the development of electrochemical HAT-related biodetection and drug discovery.

Graphical abstract

A sensitive electrochemical immunoassay for testing HAT p300 based on both graphene-assisted supported AuPd nanomaterial (AuPd@GO composite) and a typical amperometric i-t technique with fast response is developed favorably.

Keywords

Graphene-assisted supported AuPd nanomaterial Electrochemical immunoassay Histone acetylase Inhibitor Amperometric i-t curve 

Notes

Funding information

This work received financial support from the National Natural Science Foundation of China (21605089 and 81773483), the Ningbo Municipal Natural Science Foundation (2017A610231 and 2018A610217), the Open Subject of State Key Laboratory of Chemo/Biosensing and Chemometrics (2016001), and Zhejiang Provincial Natural Science Foundation of China (LGF18B070002). This work was also sponsored by K.C. Wong Magna Fund in Ningbo University.

Compliance with ethical standards

This study was approved by the Regional Ethics Committee of the Hunan Provincial People’s Hospital, and the blood and urine samples from the Hunan Provincial People’s Hospital in this study are permitted by patients through signed informed consents.

Conflict of interest

The authors declare that they have no competing interests.

Supplementary material

216_2019_2112_MOESM1_ESM.pdf (190 kb)
ESM 1 (PDF 190 kb)

References

  1. 1.
    Doll S, Burlingame AL. Mass spectrometry-based detection and assignment of protein posttranslational modifications. ACS Chem Biol. 2015;10(1):63–71.CrossRefGoogle Scholar
  2. 2.
    Casey AK, Orth K. Enzymes involved in AMPylation and deAMPylation. Chem Rev. 2018;118(3):1199–215.CrossRefGoogle Scholar
  3. 3.
    Li C, Wang LX. Chemoenzymatic methods for the synthesis of glycoproteins. Chem Rev. 2018;118(17):8359–413.CrossRefGoogle Scholar
  4. 4.
    Klein T, Eckhard U, Dufour A, Solis N, Overall CM. Proteolytic cleavage-mechanisms, function, and “Omic” approaches for a near-ubiquitous posttranslational modification. Chem Rev. 2018;118(3):1137–68.CrossRefGoogle Scholar
  5. 5.
    Ali I, Conrad RJ, Verdin E, Ott M. Lysine acetylation goes global: from epigenetics to metabolism and therapeutics. Chem Rev. 2018;118(3):1216–52.CrossRefGoogle Scholar
  6. 6.
    Kang K, Choi JM, Fox JM, Snyder PW, Moustakas DT, Whitesides GM. Acetylation of surface lysine groups of a protein alters the organization and composition of its crystal contacts. J Phys Chem B. 2016;120(27):6461–8.CrossRefGoogle Scholar
  7. 7.
    McCullough CE, Marmorstein R. Molecular basis for histone acetyltransferase regulation by binding partners, associated domains, and autoacetylation. ACS Chem Biol. 2016;11(3):632–42.CrossRefGoogle Scholar
  8. 8.
    Zou Y, Zhang HX, Wang ZH, Liu QY, Liu Y. A novel ECL method for histone acetyltransferases (HATs) activity analysis by integrating HCR signal amplification and ECL silver clusters. Talanta. 2019;198:39–44.CrossRefGoogle Scholar
  9. 9.
    Michaelides MR, Kluge A, Patane M, Van Drie JH, Wang C, Hansen TM, et al. Discovery of spiro oxazolidinediones as selective, orally bioavailable inhibitors of p300/CBP histone acetyltransferases. ACS Med Chem Lett. 2018;9(1):28–33.CrossRefGoogle Scholar
  10. 10.
    Han Z, Chou CW, Yang XK, Bartlett MG, Zheng YG. Profiling cellular substrates of lysine acetyltransferases GCN5 and p300 with orthogonal labeling and click chemistry. ACS Chem Biol. 2017;12(6):1547–55.CrossRefGoogle Scholar
  11. 11.
    Green KD, Biswas T, Pang AH, Willby MJ, Reed MS, Stuchlik O, et al. Acetylation by eis and deacetylation by Rv1151c of mycobacterium tuberculosis HupB: biochemical and structural insight. Biochemistry. 2018;57(5):781–90.CrossRefGoogle Scholar
  12. 12.
    Young IA, Mittal C, Shogren-Knaak MA. Expression and purification of histone H3 proteins containing multiple sites of lysine acetylation using nonsense suppression. Protein Expr Purif. 2016;118:92–7.CrossRefGoogle Scholar
  13. 13.
    Bonhoure A, Vallentin A, Martin M, Senff-Ribeiro A, Amson R, Telerman A, et al. Acetylation of translationally controlled tumor protein promotes its degradation through chaperone-mediated autophagy. Eur J Cell Biol. 2017;96(2):83–98.CrossRefGoogle Scholar
  14. 14.
    Bose DA, Donahue G, Reinberg D, Shiekhattar R, Bonasio R, Berger SL. RNA binding to CBP stimulates histone acetylation and transcription. Cell. 2017;168(1–2):135–49.CrossRefGoogle Scholar
  15. 15.
    Aljayyoussi G, Gumbleton M. A novel cost-effective approach for the efficient radiolabeling of dendritic macromolecules with a β-emitting radiotracer. Tetrahedron Lett. 2013;54(9):1045–8.CrossRefGoogle Scholar
  16. 16.
    Thakkar A, Wavreille AS, Pei D. Traceless capping agent for peptide sequencing by partial edman degradation and mass spectrometry. Anal Chem. 2006;78(16):5935–9.CrossRefGoogle Scholar
  17. 17.
    Baral A, Asokan A, Bauer V, Kieffer B, Torbeev V. Chemical synthesis of transactivation domain (TAD) of tumor suppressor protein p53 by native chemical ligation of three peptide segments. Tetrahedron. 2019;75(6):703–8.CrossRefGoogle Scholar
  18. 18.
    Park H, You S, Kim J, Kim W, Do J, Jang Y, et al. Seventeen O-acetylated N-glycans and six O-acetylation sites of Myozyme identified using liquid chromatography-tandem mass spectrometry. J Pharm Biomed. 2019;169:188–95.CrossRefGoogle Scholar
  19. 19.
    Felix FS, Angnes L. Electrochemical immunosensors-a powerful tool for analytical applications. Biosens Bioelectron. 2018;102:470–8.CrossRefGoogle Scholar
  20. 20.
    Wen W, Yan X, Zhu CZ, Du D, Lin YH. Recent advances in electrochemical immunosensors. Anal Chem. 2017;89(1):138–56.CrossRefGoogle Scholar
  21. 21.
    Liu YB, Xu LP, Wang SQ, Yang WZ, Wen YQ, Zhang XJ. An ultrasensitive electrochemical immunosensor for apolipoprotein E4 based on fractal nanostructures and enzyme amplification. Biosens Bioelectron. 2015;71:396–400.CrossRefGoogle Scholar
  22. 22.
    Yu ZZ, Tang Y, Cai GN, Ren RR, Tang DP. Paper electrode-based flexible pressure sensor for point-of-care immunoassay with digital multimeter. Anal Chem. 2019;91:1222–6.CrossRefGoogle Scholar
  23. 23.
    Zeng RJ, Luo ZB, Zhang LJ, Tang DP. Platinum nanozyme-catalyzed gas generation for pressure-based bioassay using polyaniline nanowires-functionalized graphene oxide framework. Anal Chem. 2018;90:12299–306.CrossRefGoogle Scholar
  24. 24.
    Pang PF, Teng X, Chen M, Zhang YL, Wang HB, Yang C, et al. Ultrasensitive enzyme-free electrochemical immunosensor for microcystin-LR using molybdenum disulfide/gold nanoclusters nanocomposites as platform and Au@Pt core-shell nanoparticles as signal enhancer. Sensors Actuators B Chem. 2018;266:400–7.CrossRefGoogle Scholar
  25. 25.
    Tang QR, Zhang LH, Tan XF, Jiao L, Wei Q, Li H. Bioinspired synthesis of organic-inorganic hybrid nanoflowers for robust enzyme-free electrochemical immunoassay. Biosens Bioelectron. 2019;133:94–9.CrossRefGoogle Scholar
  26. 26.
    Fu Y, Xu P, Huang D, Zeng G, Lai C, Qin L, et al. Au nanoparticles decorated on activated coke via a facile preparation for efficient catalytic reduction of nitrophenols and azo dyes. Appl Surf Sci. 2019;473:578–88.CrossRefGoogle Scholar
  27. 27.
    Zhang Z, Shi H, Wu Q, Bu X, Yang Y, Zhang J. Hierarchical structure based on Au nanoparticles and porous CeO2 nanorods: enhanced activity for catalytic applications. Mater Lett. 2019;242:20–3.CrossRefGoogle Scholar
  28. 28.
    Zeng RJ, Luo ZB, Su LS, Zhang LJ, Tang DP, Niessner R, et al. Palindromic molecular beacon based Z-scheme BiOCl-Au-CdS photoelectrochemical biodetection. Anal Chem. 2019;91:2447–54.CrossRefGoogle Scholar
  29. 29.
    Mandal R, Baranwal A, Srivastava A, Chandra P. Evolving trends in bio/chemical sensor fabrication incorporating bimetallic nanoparticles. Biosens Bioelectron. 2018;117:546–61.CrossRefGoogle Scholar
  30. 30.
    Chen X, Shen Y, Zhou P, Zhong X, Li G, Han C, et al. Bimetallic Au/Pd nanoparticles decorated ZnO nanowires for NO2 detection. Sensors Actuators B Chem. 2019;289:160–8.CrossRefGoogle Scholar
  31. 31.
    Xia H, An J, Hong M, Xu S, Zhang L, Zuo S. Aerobic oxidation of 5-hydroxymethylfurfural to 2,5-difurancarboxylic acid over Pd-Au nanoparticles supported on Mg-Al hydrotalcite. Catal Today. 2019;319:113–20.CrossRefGoogle Scholar
  32. 32.
    Zhang Y, Gao F, Fu ML. Composite of Au-Pd nanoalloys/reduced graphene oxide toward catalytic selective organic transformation to fine chemicals. Chem Phys Lett. 2018;691:61–7.CrossRefGoogle Scholar
  33. 33.
    Hatamluyi B, Lorestani F, Es’haghi Z. Au/Pd@rGO nanocomposite decorated with poly (L-cysteine) as a probe for simultaneous sensitive electrochemical determination of anticancer drugs, ifosfamide and etoposide. Biosens Bioelectron. 2018;120:22–9.CrossRefGoogle Scholar
  34. 34.
    Raghavendra P, Reddy GV, Sivasubramanian R, Chandana PS, Sarma LS. Reduced graphene oxide-supported Pd@Au bimetallic nano electrocatalyst for enhanced oxygen reduction reaction in alkaline media. Int J Hydrog Energy. 2018;43(8):4125–35.CrossRefGoogle Scholar
  35. 35.
    Cai GN, Yu ZZ, Ren RR, Tang DP. Exciton-plasmon interaction between AuNPs/graphene nanohybrids and CdS quantum dots/TiO2 for photoelectrochemical aptasensing of prostate-specific antigen. ACS Sens. 2018;3:632–9.CrossRefGoogle Scholar
  36. 36.
    Tahriri M, Monico MD, Moghanian A, Yaraki MT, Torres R. Yadegari, graphene and its derivatives: opportunities and challenges in dentistry. Mater Sci Eng C Mater. 2019;102:171–85.CrossRefGoogle Scholar
  37. 37.
    Wang J, Jin X, Li C, Wang W, Wu H, Guo S. Graphene and graphene derivatives toughening polymers: toward high toughness and strength. Chem Eng J. 2019;370:831–54.CrossRefGoogle Scholar
  38. 38.
    Vashist SK, Luppa PB, Yeo LY, Ozcan A, Luong JHT. Emerging technologies for next-generation point-of-care testing. Trends Biotechnol. 2015;33:692–705.CrossRefGoogle Scholar
  39. 39.
    Hu YF, Chen SY, Han YT, Chen HJ, Wang Q, Nie Z, et al. Unique electrocatalytic activity of a nucleic acid-mimicking coordination polymer for the sensitive detection of coenzyme A and histone acetyltransferase activity. Chem Commun. 2015;51:17611–4.CrossRefGoogle Scholar
  40. 40.
    Yang HM, Zhang Y, Li L, Sun GQ, Zhang LN, Ge SG, et al. Real-time and in situ enzyme inhibition assay for the flux of hydrogen sulfide based on 3D interwoven AuPd-reduced graphene oxide network. Biosens Bioelectron. 2017;87:53–8.CrossRefGoogle Scholar
  41. 41.
    Li J, Tang W, Huang J, Jin J, Ma J. Polyethyleneimine decorated graphene oxide-supported Ni1-xFex bimetallic nanoparticles as efficient and robust electrocatalysts for hydrazine fuel cells. Catal Sci Technol. 2013;3:3155–62.CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Clinical Laboratory of Hunan Provincial People’s HospitalThe First Affiliated Hospital of Hunan Normal UniversityChangshaChina
  2. 2.Blood Transfusion DepartmentXiangya Hospital of Central South UniversityChangshaChina
  3. 3.Faculty of Materials Science and Chemical EngineeringNingbo UniversityNingboChina
  4. 4.State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical EngineeringHunan UniversityChangshaChina

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