Skip to main content

Surface Plasmon Resonance Imaging-Mass Spectrometry Coupling on Antibody Array Biochip: Multiplex Monitoring of Biomolecular Interactions and On-Chip Identification of Captured Antigen

  • Protocol
  • First Online:

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2237))

Abstract

The coupling of surface plasmon resonance imaging (SPRi) with mass spectrometry (MS) offers a very promising multidimensional analysis. This system takes advantage of the two well-established techniques: SPR, which allows for the analysis of biomolecular interactions through the determination of kinetic and thermodynamic constants, and MS, which can characterize biological structures from mass measurements and fragmentation experiments. Here, a protocol for the coupling of SPRi with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is described using a biochip grafted by antibodies in an array format. Interaction between β-lactoglobulin antibodies and the protein antigen is detected and analyzed by SPRi. Then, the arrayed biochip which fitted a commercially MALDI target was inserted in a MALDI source, and mass spectra were recorded directly from the biochip surface from each antibody spot, showing protein ions attributed to the corresponding specific protein antigens.

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

Buying options

Protocol
USD   49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   99.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   129.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   199.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Springer Nature is developing a new tool to find and evaluate Protocols. Learn more

References

  1. Karlsson R, Michaelsson A, Mattsson L (1991) Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J Immunol Methods 145(229–240):229–240

    Article  CAS  Google Scholar 

  2. Homola J (2003) Present and future of surface plasmon resonance biosensors. Anal Bioanal Chem 377(3):528–539

    Article  CAS  Google Scholar 

  3. Wassaf D et al (2006) High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays. Anal Biochem 351(2):241–253

    Article  CAS  Google Scholar 

  4. Homola J (2008) Surface plasmon resonance sensors for detection of chemical and biological species. Chem Rev 108(2):462–493

    Article  CAS  Google Scholar 

  5. Nogues C, Leh H, Langendorf CG, Law RHP, Buckle AM, Buckle M (2010) Characterisation of peptide microarrays for studying antibody-antigen binding using surface plasmon resonance imagery. PLoS One 5(8):1–7

    Article  Google Scholar 

  6. Nogues C, Leh H, Lautru J, Delelis O, Buckle M (2012) Efficient antifouling surface for quantitative surface plasmon resonance based biosensor analysis. PLoS One 7(9):e44287

    Article  CAS  Google Scholar 

  7. Nedelkov D, Nelson RW (2001) Analysis of native proteins from biological fluids by biomolecular interaction analysis mass spectrometry (BIA/MS): exploring the limit of detection, identification of non-specific binding and detection of multi-protein complexes. Biosens Bioelectron 16(9–12):1071–1078

    Article  CAS  Google Scholar 

  8. Gilligan JJ, Schuck P, Yergey AL (2002) Mass spectrometry after capture and small-volume elution of analyte from a surface plasmon resonance biosensor. Anal Chem 74(9):2041–2047

    Article  CAS  Google Scholar 

  9. Boireau W, Rouleau A, Lucchi G, Ducoroy P (2009) Revisited BIA-MS combination: entire ‘on-a-chip’ processing leading to the proteins identification at low femtomole to sub-femtomole levels. Biosens Bioelectron 24(5):1121–1127

    Article  CAS  Google Scholar 

  10. Xue J, Bai Y, Liu H (2019) Hybrid methods of surface plasmon resonance coupled to mass spectrometry for biomolecular interaction analysis. Anal Bioanal Chem 411(17):3721–3729

    Article  CAS  Google Scholar 

  11. Krone JR, Nelson RW, Dogruel D, Williams P, Granzow R (1997) BIA/MS: interfacing biomolecular interaction analysis with mass spectrometry. Anal Biochem 244(1):124–132

    Article  CAS  Google Scholar 

  12. Jansson Ö, Larsericsdotter H, Zhukov A, Areskoug D, Oscarsson S, Buijs J (2006) Optimizing the surface plasmon resonance/mass spectrometry interface for functional proteomics applications: how to avoid and utilize nonspecific adsorption. Proteomics 6:2355–2364

    Article  Google Scholar 

  13. Bouffartigues E, Leh H, Anger-Leroy M, Rimsky S, Buckle M (2007) Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions. Nucleic Acids Res 35(6):e39

    Article  Google Scholar 

  14. Stigter ECA, de Jong GJ, van Bennekom WP (2009) Development of an on-line SPR-digestion-nanoLC-MS/MS system for the quantification and identification of interferon-γ in plasma. Biosensor Bioelectron 24(7):2184–2190

    Article  CAS  Google Scholar 

  15. Zhang Y et al (2015) Interface for online coupling of surface plasmon resonance to direct analysis in real time mass spectrometry. Anal Chem 87(13):6505–6509

    Article  CAS  Google Scholar 

  16. Joshi S, Zuilhof H, van Beek TA, Nielen MWF (2017) Biochip spray: simplified coupling of surface plasmon resonance biosensing and mass spectrometry. Anal Chem 89(3):1427–1432

    Article  CAS  Google Scholar 

  17. Nedelkov D (2007) Development of surface plasmon resonance mass spectrometry array platform. Anal Chem 79(15):5987–5990

    Article  CAS  Google Scholar 

  18. Bellon S et al (2009) Hyphenation of surface plasmon resonance imaging to matrix-assisted laser desorption ionization mass spectrometry by on-chip mass spectrometry and tandem mass spectrometry analysis. Anal Chem 81(18):7695–7702

    Article  CAS  Google Scholar 

  19. Remy-Martin F et al (2012) Automated cancer marker characterization in human plasma using SUrface PLASMON Resonance in Array combined with Mass Spectrometry (SUPRA-MS). Procedia Chem 6:11–19

    Article  CAS  Google Scholar 

  20. Stigter ECA, de Jong GJ, van Bennekom WP (2013) Coupling surface-plasmon resonance and mass spectrometry to quantify and to identify ligands. TrAC—Trends Anal Chem 45:107–120

    Article  CAS  Google Scholar 

  21. Musso J et al (2015) Biomarkers probed in saliva by surface plasmon resonance imaging coupled to matrix-assisted laser desorption/ionization mass spectrometry in array format. Anal Bioanal Chem 407(5):1285–1294

    Article  CAS  Google Scholar 

  22. Przybylski C et al (2020) Surface plasmon resonance imaging coupled to on-chip mass spectrometry: a new tool to probe protein-GAG interactions. Anal Bioanal Chem 412:507–519

    Google Scholar 

Download references

Acknowledgments

Authors are indebted to Dr. D. Lebeau for access to the MALDI-TOF/TOF MS instrument (Den-Service d’Etude du Comportement des Radionucléides, CEA, Paris-Saclay University, France); A. H. acknowledges fellowships from Université d’Evry—Paris Saclay and Région Ile-de France (Dim Analytics).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Régis Daniel .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2021 Springer Science+Business Media, LLC, part of Springer Nature

About this protocol

Check for updates. Verify currency and authenticity via CrossMark

Cite this protocol

Halushkina, A., Buchmann, W., Jarroux, N., Daniel, R. (2021). Surface Plasmon Resonance Imaging-Mass Spectrometry Coupling on Antibody Array Biochip: Multiplex Monitoring of Biomolecular Interactions and On-Chip Identification of Captured Antigen. In: Whittaker, K.C., Huang, RP. (eds) Antibody Arrays. Methods in Molecular Biology, vol 2237. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1064-0_5

Download citation

  • DOI: https://doi.org/10.1007/978-1-0716-1064-0_5

  • Published:

  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1063-3

  • Online ISBN: 978-1-0716-1064-0

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics