Skip to main content
SpringerLink
Log in

Tyrosine-Phosphorylated Peptide Imprinted Particles Prepared by Reversible Addition–Fragmentation Chain Transfer Polymerization and “Epitope” Strategy: Selective Recognition of Phosphorylated Angiotensin II

  • Original
  • Published:
Chromatographia Aims and scope Submit manuscript

Abstract

Phosphorylation is one of the most common post-translational modifications of proteins. Recognition of phosphorylated peptides with high selectivity is an important prerequisite for the structural identification of protein phosphorylation. By the application of molecular imprinting technology, a kind of tyrosine-phosphorylated peptide imprinted particles was prepared by the combination of reversible addition-fragmentation chain transfer (RAFT) polymerization and “epitope” strategy that applied in tyrosine-phosphorylated peptides recognition. Phenylphosphonic acid was used as the dummy template of the phosphorylated angiotensin II, which was one of the natural tyrosine-phosphorylated peptides. After the template modified by hydrogen bond with ureidopropyl group on the surface of silica, the surface imprinted particles with controlled and imprinted shell were synthesized by radical polymerization with RAFT strategy. The imprinted particles were obtained after the peptide removed and dithioester group destructed under alkaline condition. The binding capacity of phenylphosphonic acid reached 0.198 mg g−1 with imprinting factor (IF) as 2.70, while the binding capacity of phosphorylated angiotensin II reached 0.792 mg g−1 with IF as 1.96, which were obviously higher than with IF of that without RAFT strategy. Furthermore, phosphorylated angiotensin II could be selectively recognized by the imprinted particles even in presence of angiotensin II without phosphorylated. The performance of the phosphopeptide recognition remained 92% after five cycles of adsorption and desorption. All these results demonstrated that the tyrosine-phosphorylated imprinted particles prepared by combing RAFT polymerization and “epitope” strategy are promising to achieve the phosphopeptide recognition with higher recognition ability, selectivity and reusability.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig.4
Fig.5
Fig.6
Fig.7
Fig.8
Fig.9
Fig.10
Fig. 11

Similar content being viewed by others

Data Availability

No datasets were generated or analysed during the current study.

References

  1. Doyle HA, Mamula MJ (2001) Post-translational protein modifications in antigen recognition and autoimmunity. Trends Immunol 22:443–449. https://doi.org/10.1016/s1471-4906(01)01976-7

    Article  CAS  PubMed  Google Scholar 

  2. Demmers JAA, van der Wal L, Bezstarosti K (2020) Detection of protein ubiquitination sites by peptide enrichment and mass spectrometry. J Vis Exp. https://doi.org/10.3791/59079

    Article  PubMed  Google Scholar 

  3. Hauser A, Penkert M, Hackenberger CPR (2017) Chemical approaches to investigate labile peptide and protein phosphorylation. Acc Chem Res 50:1883–1893. https://doi.org/10.1021/acs.accounts.7b00170

    Article  CAS  PubMed  Google Scholar 

  4. Huang BL, Liu Y, Yao HW, Zhao Y (2020) NMR-based investigation into protein phosphorylation. Int J Biol Macromol 145:53–63. https://doi.org/10.1016/j.ijbiomac.2019.12.171

    Article  CAS  PubMed  Google Scholar 

  5. Franciosa G, Martinez-Val A, Olsen JV (2020) Deciphering the human phosphoproteome. Nat Biotechnol 38:285–286. https://doi.org/10.1038/s41587-020-0441-3

    Article  CAS  PubMed  Google Scholar 

  6. Lafite P, Daniellou R (2012) Rare and unusual glycosylation of peptides and proteins. Nat Prod Rep 29:729–738. https://doi.org/10.1039/c2np20030a

    Article  CAS  PubMed  Google Scholar 

  7. Chatterjee J, Rechenmacher F, Kessler H (2013) N-methylation of peptides and proteins: an important element for modulating biological functions. Angew Chem Int Ed 52:254–269. https://doi.org/10.1002/anie.201205674

    Article  CAS  Google Scholar 

  8. Wang YY, Yao J, Yang PY, Deng C, Fan H (2012) Immobilization of antibodies on magnetic carbonaceous microspheres for selective enrichment of lysine-acetylated proteins and peptides. Chin J Chem 30:2549–2555. https://doi.org/10.1002/cjoc.201200542

    Article  CAS  Google Scholar 

  9. Delom F, Chevet E (2006) Phosphoprotein analysis: from proteins to proteomes. Proteome Sci 4:1–15. https://doi.org/10.1186/1477-5956-4-15

    Article  CAS  Google Scholar 

  10. Hunter T (2000) Signaling—2000 and beyond. Cell 100:113–127. https://doi.org/10.1016/S0092-8674(00)81688-8

    Article  CAS  PubMed  Google Scholar 

  11. Eyrich B, Sickmann A, Zahedi RP (2011) Catch me if you can: mass spectrometry-based phosphoproteomics and quantification strategies. Proteomics 11:554–570. https://doi.org/10.1002/pmic.201000489

    Article  CAS  PubMed  Google Scholar 

  12. Swaney DL, Villén J (2016) Enrichment of phosphopeptides via immobilized metal affinity chromatography. Cold Spring Harb Protoc 2016:88005. https://doi.org/10.1101/pdb.prot088005

    Article  Google Scholar 

  13. Diez IA, Govender I, Naicker P, Stoychev S, Jordaan J, Jensen ON (2021) Zirconium(IV)-IMAC revisited: improved performance and phosphoproteome coverage by magnetic microparticles for phosphopeptide affinity enrichment. J Proteome Res 20:453–462. https://doi.org/10.1021/acs.jproteome.0c00508

    Article  CAS  Google Scholar 

  14. Ruprecht B, Koch H, Domasinska P, Frejno M, Kuster B, Lemeer S (2017) Optimized enrichment of phosphoproteomes by Fe-IMAC column chromatography. Methods Mol Biol 1550:47–60. https://doi.org/10.1007/978-1-4939-6747-6_5

    Article  CAS  PubMed  Google Scholar 

  15. Cernigoj U, Gaspersic J, Fichtenbaum A, Lendero Krajnc N, Vidic J, Mitulovic G, Strancar A (2016) Titanium dioxide nanoparticle coating of polymethacrylate-based chromatographic monoliths for phosphopetides enrichment. Anal Chim Acta 942:146–154. https://doi.org/10.1016/j.aca.2016.08.044

    Article  CAS  PubMed  Google Scholar 

  16. Chen YM, Hoehenwarter W (2019) Rapid and reproducible phosphopeptide enrichment by tandem metal oxide affinity chromatography: application to boron deficiency induced phosphoproteomics. Plant J 98:370–384. https://doi.org/10.1111/tpj.14215

    Article  CAS  PubMed  Google Scholar 

  17. Mirza MR, Rainer M, Guzel Y, Choudhary IM, Bonn GK (2012) A novel strategy for phosphopeptide enrichment using lanthanide phosphate co-precipitation. Anal Bioanal Chem 404:853–862. https://doi.org/10.1007/s00216-012-6215-0

    Article  CAS  PubMed  Google Scholar 

  18. Han GH, Ye ML, Zhou HJ, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J (2008) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics 8:1346–1361. https://doi.org/10.1002/pmic.200700884

    Article  CAS  PubMed  Google Scholar 

  19. Hu YC, Li Y, Gao H, Jiang B, Zhang X, Li X, Wu Q, Liang Z, Zhang L, Zhang Y (2019) Cleavable hydrophobic derivatization strategy for enrichment and identification of phosphorylated lysine peptides. Anal Bioanal Chem 411:4159–4166. https://doi.org/10.1007/s00216-019-01770-w

    Article  CAS  PubMed  Google Scholar 

  20. Bijttebier S, Theunis C, Jahouh F, Martins DR, Verhemeldonck M, Grauwen K, Dillen L, Mercken M (2021) Development of immunoprecipitation-two-dimensional liquid chromatography-mass spectrometry methodology as biomarker read-out to quantify phosphorylated tau in cerebrospinal fluid from Alzheimer disease patients. J Chromatogr A 1651:462299. https://doi.org/10.1016/j.chroma.2021.462299

    Article  CAS  PubMed  Google Scholar 

  21. Hunter T (2015) Discovering the first tyrosine kinase. Proc Natl Acad Sci USA 112:7877–7882. https://doi.org/10.1073/pnas.1508223112

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  22. Xu L, Hu YF, Shen F, Li Q, Ren X (2013) Specific recognition of tyrosine-phosphorylated peptides by epitope imprinting of phenylphosphonic acid. J Chromatogr A 1293:85–91. https://doi.org/10.1016/j.chroma.2013.04.013

    Article  CAS  PubMed  Google Scholar 

  23. Yang XQ, Xia Y (2016) Selective enrichment and separation of phosphotyrosine peptides by thermosensitive molecularly imprinted polymers. J Sep Sci 39:419–426. https://doi.org/10.1002/jssc.201501063

    Article  CAS  PubMed  Google Scholar 

  24. Duarte M, Subedi P, Yilmaz E, Marcus K, Laurell T, Ekstrom S (2018) Molecularly imprinted polymers synthesized via template immobilization on fumed silica nanoparticles for the enrichment of phosphopeptides. J Mol Recognit 31:2677. https://doi.org/10.1002/jmr.2677

    Article  CAS  Google Scholar 

  25. Rachkov A, Minoura N (2001) Towards molecularly imprinted polymers selective to peptides and proteins. The epitope approach. Biochim et Biophys Acta (BBA)-Protein Struct Mol Enzymol 1544:255–266. https://doi.org/10.1016/s0167-4838(00)00226-0

    Article  CAS  Google Scholar 

  26. Yang K, Li S, Liu L, Chen Y, Zhou W, Pei J, Liang Z, Zhang L, Zhang Y (2019) Epitope imprinting technology: progress, applications, and perspectives toward artificial antibodies. Adv Mater 31:e1902048. https://doi.org/10.1002/adma.201902048

    Article  CAS  PubMed  Google Scholar 

  27. Li Q, Shen F, Zhang X, Hu Y, Zhang Q, Xu L, Ren X (2013) One-pot synthesis of phenylphosphonic acid imprinted polymers for tyrosine phosphopeptides recognition in aqueous phase. Anal Chim Acta 795:82–87. https://doi.org/10.1016/j.aca.2013.07.040

    Article  CAS  PubMed  Google Scholar 

  28. Liu QS, Zhang KN, Jin YH, Wang X, Liu Y, Liu H, Xie M (2018) Phosphate-imprinted magnetic nanoparticles using phenylphosphonic acid as a template for excellent recognition of tyrosine phosphopeptides. Talanta 186:346–353. https://doi.org/10.1016/j.talanta.2018.04.025

    Article  CAS  PubMed  Google Scholar 

  29. Zhang G, Jiang L, Zhou J, Hu L, Feng S (2019) Epitope-imprinted mesoporous silica nanoparticles for specific recognition of tyrosine phosphorylation. Chem Commun 55:9927–9930. https://doi.org/10.1039/c9cc03950c

    Article  CAS  Google Scholar 

  30. Rouhi M, Incel A, Shinde S (2021) Role of comonomers in the recognition of anionic biomolecules in water: hydrogen-bonded imprinted polymeric receptor. ACS Appl Polymer Mater 3:4904–4912. https://doi.org/10.1021/acsapm.1c00685

    Article  CAS  Google Scholar 

  31. Chiefari J, Chong YKB, Ercole F, Julia K (1998) Living free-radical polymerization by reversible addition−fragmentation chain transfer: the RAFT process. Macromolecules 31:5559–5562. https://doi.org/10.1021/ma9804951

    Article  CAS  Google Scholar 

  32. Thang SH, Chong BYK, Mayadunne RTA, Moad G, Rizzardo E (1999) A novel synthesis of functional dithioesters, dithiocarbamates, xanthates and trithiocarbonates. Tetrahedron Lett 40:2435–2438. https://doi.org/10.1016/s0040-4039(99)00177-x

    Article  CAS  Google Scholar 

  33. Li QR, Yang KG, Liang Y, Jiang B, Liu J, Zhang L, Liang Z, Zhang Y (2014) Surface protein imprinted core-shell particles for high selective lysozyme recognition prepared by reversible addition-fragmentation chain transfer strategy. ACS Appl Mater Interfaces 6:21954–21960. https://doi.org/10.1021/am5072783

    Article  CAS  PubMed  Google Scholar 

  34. Chen FF, Wang JY, Lu RC, Chen H, Xie X (2018) Fast and high-efficiency magnetic surface imprinting based on microwave-accelerated reversible addition fragmentation chain transfer polymerization for the selective extraction of estrogen residues in milk. J Chromatogr A 1562:19–26. https://doi.org/10.1016/j.chroma.2018.05.047

    Article  CAS  PubMed  Google Scholar 

  35. Kusrini E, Yusof NF, Mehamod FS, Suah FBM, Juwono FH, Yatim A, Setiawan EA (2018) The effect of RAFT polymerization on the physical properties of thiamphenicol-imprinted polymer. E3S Web Conf 67:2267–1242. https://doi.org/10.1051/e3sconf/20186703050

    Article  CAS  Google Scholar 

  36. Kislenko E, İncel A, Gawlitza K, Sellergren B, Rurack K (2023) Towards molecularly imprinted polymers that respond to and capture phosphorylated tyrosine epitopes using fluorescent bis-urea and bis-imidazolium receptors. J Mater Chem B 11:10873–10882. https://doi.org/10.1039/d3tb01474f

    Article  CAS  PubMed  Google Scholar 

  37. Min Y, Jiang B, Wu C, Xia SM, Zhang XD, Liang Z, Zhang LH, Zhang YK (2014) 1.9 μm superficially porous packing material with radially oriented pores and tailored pore size for ultra-fast separation of small molecules and biomolecules. J Chromatogr A 1356:148–156. https://doi.org/10.1016/j.chroma.2014.06.049

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgements

This work was supported by National Natural Science Foundation of China (No. 21804099).

Funding

This work was funded by National Natural Science Foundation of China (Grant Number 21804099). Yongjian Wang, Nurimangul Muntiza, Wenbin Zhang, Qinran Li and Hongfeng Zhang declared that the funds were supported by National Natural Science Foundation of China (Grant Number 21804099). Qiliang Deng declared that there was no fund support in the research process. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

Author information

Authors and Affiliations

  1. College of Chemical Engineering and Materials Science, Tianjin University of Science and Technology, 300457, Tianjin, People’s Republic of China

    Yongjian Wang, Wenbin Zhang, Hongfeng Zhang, Qinran Li & Qiliang Deng

  2. College of Science, Tianjin University of Science and Technology, 300457, Tianjin, People’s Republic of China

    Nurimangul Muntiza, Qinran Li & Qiliang Deng

  3. State Key Laboratory of Biobased Fiber Manufacturing Technology, Tianjin University of Science and Technology, 300457, Tianjin, People’s Republic of China

    Hongfeng Zhang

  4. Tianjin Key Laboratory of Multiplexed Identification for Port Hazardous Chemicals, Tianjin University of Science and Technology, 300457, Tianjin, People’s Republic of China

    Qinran Li & Qiliang Deng

Authors
  1. Yongjian Wang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Nurimangul Muntiza
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Wenbin Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Hongfeng Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Qinran Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Qiliang Deng
    View author publications

    You can also search for this author in PubMed Google Scholar

Contributions

Yongjian Wang, Nurimangul Muntiza and Wenbin Zhang proceed the main experiment and wrote the main manuscript text. Hongfeng Zhang established chromatographic separation methods and provided support for the use of chromatographic instruments. Dr. Qinran Li revised the whole manuscript and fnished the final draft. Prof. Qiliang Deng put forward some useful suggestions for the revision and improvement of the manuscript. All of the authors reviewed the manuscript.

Corresponding author

Correspondence to Qinran Li.

Ethics declarations

Conflict of Interest

The authors declare no competing interests.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Supplementary Information

Below is the link to the electronic supplementary material.

Supplementary file1 (DOCX 120 KB)

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Wang, Y., Muntiza, N., Zhang, W. et al. Tyrosine-Phosphorylated Peptide Imprinted Particles Prepared by Reversible Addition–Fragmentation Chain Transfer Polymerization and “Epitope” Strategy: Selective Recognition of Phosphorylated Angiotensin II. Chromatographia (2024). https://doi.org/10.1007/s10337-024-04340-0

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • DOI: https://doi.org/10.1007/s10337-024-04340-0

Keywords

Search

Navigation