Skip to main content

Determination of Kinetic Data Using Surface Plasmon Resonance Biosensors

  • Protocol
Molecular Diagnosis of Infectious Diseases

Part of the book series: Methods in Molecular Medicineā„¢ ((MIMM,volume 94))

Abstract

The use of biosensors employing surface plasmon resonance (SPR) provides excellent instrumentation for a label-free, real-time investigation of biomolecular interactions. A broad range of biological applications including antibody-antigen interactions can be analyzed. One major advantage of kinetic analysis using SPR-based biosensors is the option of determining separately distinct association and dissociation rate constants exceeding the classical steady-state analysis of biomolecules. Based on these data new possibilities for drug design, characterizing human pathogens, and the development of therapeutic antibodies can be achieved. The hardware of commercially available systems is described, practical step by step procedures are given, and possibilities and limitations of the technology are discussed.

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

Access this chapter

Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 89.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 119.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
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

Institutional subscriptions

References

  1. Rich, R. L. and Myszka, D. G. (2001) Survey of the year 2000 commercial optical biosensor literature. J. Mol. Recognit. 14, 273ā€“294s.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  2. Wink, T., de Beer, J., Hennink, W. E., Bult, A., and van Bennekom, W. P. (1999) Interaction between plasmid DNA and cationic polymers studied by surface plasmon resonance spectrometry. Anal. Chem. 71, 801ā€“805.

    ArticleĀ  CASĀ  Google ScholarĀ 

  3. Baird, C. L. and Myszka, D. G. (2001) Current and emerging commercial optical biosensors. J. Mol. Recognit. 14, 261ā€“268.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  4. Stenberg, E., Persson, B., Roos, H., and Urbaniczky, C. (1991) Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J. Colloid Interface Sci. 143, 513ā€“526.

    ArticleĀ  CASĀ  Google ScholarĀ 

  5. Kovacs, G. D. (1982) In Electromagnetic Surface Modes (Boardman, A. D., ed.), Wiley, New York, p. 143.

    Google ScholarĀ 

  6. Zimmermann, B., Hahnefeld, C., and Herberg, F. W. (2002) Applications of biomolecular interaction analysis in drug development. TARGETS 1, 66ā€“73.

    ArticleĀ  CASĀ  Google ScholarĀ 

  7. Jokiranta, T. S., Westin, J., Nilsson, U. R., et al. (2001) Complement C3b interactions studied with surface plasmon resonance technique. Int. Immunopharmacol. 1, 495ā€“506s.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  8. Jokiranta, T. S., Hellwage, J., Koistinen, V., Zipfel, P. F., and Meri, S. (2000) Each of the three binding sites on complement factor H interacts with a distinct site on C3b. J. Biol. Chem. 275, 27,657ā€“27,662.

    PubMedĀ  CASĀ  Google ScholarĀ 

  9. Jarva, H., Janulczyk, R., Hellwage, J., Zipfel, P. F., Bjorck, L., and Meri, S. (2002) Streptococcus pneumoniae evades complement attack and opsonophagocytosis by expressing the pspC locus-encoded Hic protein that binds to short consensus repeats 8-11 of factor H. J. Immunol. 168, 1886ā€“1894.

    PubMedĀ  CASĀ  Google ScholarĀ 

  10. Hellwage, J., Meri, T., Heikkila, T., et al. (2001) The complement regulator factor H binds to the surface protein OspE of Borrelia burgdorferi. J. Biol. Chem. 276, 8427ā€“8435.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  11. Meri, T., Hartmann, A., Lenk, D., et al. (2002) The yeast Candida albicans binds complement regulators factor H and FHL-1. Infect. Immun. 70, 5185ā€“5192.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  12. Sidobre, S., Puzo, G., and Riviere, M. (2002) Lipid-restricted recognition of mycobacterial lipoglycans by human pulmonary surfactant protein A: a surface-plasmon-resonance study. Biochem. J. 365, 89ā€“97.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  13. Jongerius-Gortemaker, B. G., Goverde, R. L., van Knapen, F., and Bergwerff, A. A. (2002) Surface plasmon resonance (BIACORE) detection of serum antibodies against Salmonella enteritidis and Salmonella typhimurium. J. Immunol. Methods 266, 33ā€“44.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  14. Hifumi, E., Kubota, N., Niimi, Y., Shimizu, K., Egashira, N., and Uda, T. (2002) Elimination of ingredients effect to improve the detection of anti HIV-1 p24 antibody in human serum using SPR apparatus. Anal. Sci. 18, 863ā€“867.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  15. McLaurin, J., Cecal, R., Kierstead, M. E., et al. (2002) Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4ā€“10 and inhibit cytotoxicity and fibrillogenesis. Nat. Med. 8, 1263ā€“1269.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  16. Gonzales, N. R., Schuck, P., Schlom, J., and Kashmiri, S. V. (2002) Surface plasmon resonance-based competition assay to assess the sera reactivity of variants of humanized antibodies. J. Immunol. Methods 268, 197ā€“210.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  17. Alaedini, A. and Latov, N. (2001) A surface plasmon resonance biosensor assay for measurement of anti-GM(1) antibodies in neuropathy. Neurology 56, 855ā€“860.

    PubMedĀ  CASĀ  Google ScholarĀ 

  18. Herberg, F. W. and Zimmermann, B. (1999) Analysis of protein kinase interactions using biomolecular interaction analysis, in Protein Phosphorylationā€”A Practical Approach (Hardie, D. G., ed.), vol. 2, Oxford University Press, Oxford, pp. 335ā€“371.

    Google ScholarĀ 

  19. Myszka, D. G. (2000) Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE. Methods Enzymol. 323, 325ā€“340.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  20. Karlsson, R. and Falt, A. (1997) Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200, 121ā€“133.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  21. Hall, D. R., Gorgani, N. N., Altin, J. G., and Winzor, D. J. (1997) Theoretical and experimental considerations of the pseudo-first-order approximation in conventional kinetic analysis of IAsys biosensor data. Anal. Biochem. 253, 145ā€“155.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  22. Oā€™Shannessy, D. J. and Winzor, D. J. (1996) Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology. Anal. Biochem. 236, 275ā€“283.

    ArticleĀ  Google ScholarĀ 

  23. Hall, D. R., Cann, J. R., and Winzor, D. J. (1996) Demonstration of an upper limit to the range of association rate constants amenable to study by biosensor technology based on surface plasmon resonance. Anal. Biochem. 235, 175ā€“184.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  24. Schuck, P. and Minton, A. P. (1996) Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. Anal. Biochem. 240, 262ā€“272.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  25. Natsume, T., Nakayama, H., and Isobe, T. (2001) BIA-MS-MS: biomolecular interaction analysis for functional proteomics. Trends Biotechnol. 19(10 suppl), S28ā€“33.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  26. Cain, K. D., Jones, D. R., and Raison, R. L. (2002) Antibody-antigen kinetics following immunization of rainbow trout (Oncorhynchus mykiss) with a T-cell dependent antigen. Dev. Comp. Immunol. 26, 181ā€“190.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  27. Ciolkowski, M. L., Fang, M. M., and Lund, M. E. (2000) A surface plasmon resonance method for detecting multiple modes of DNA-ligand interactions. J. Pharm. Biomed. Anal. 22, 1037ā€“1045.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  28. Schindler, J. F., Godbey, A., Hood, W. F., et al. (2002) Examination of the kinetic mechanism of mitogen-activated protein kinase activated protein kinase-2. Biochim. Biophys. Acta 1598, 88ā€“97.

    PubMedĀ  CASĀ  Google ScholarĀ 

  29. Hoffman, T. L., Canziani, G., Jia, L., Rucker, J., and Doms, R. W. (2000) A biosensor assay for studying ligand-membrane receptor interactions: binding of antibodies and HIV-1 Env to chemokine receptors. Proc. Natl. Acad. Sci. USA 97, 11,215ā€“11,220.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  30. Hwang, J., Fauzi, H., Fukuda, K., et al. (2000) The RNA aptamer-binding site of hepatitis C virus NS3 protease. Biochem. Biophys. Res. Commun. 279, 557ā€“562.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  31. Kamionka, A. and Dahl, M. K. (2001) Bacillus subtilis contains a cyclodextrin-binding protein which is part of a putative ABC-transporter. FEMS Microbiol. Lett. 204, 55ā€“60.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  32. Baird, C. L., Courtenay, E. S., and Myszka, D. G. (2002) Surface plasmon resonance characterization of drug/liposome interactions. Anal. Biochem. 310, 93ā€“99.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  33. Satoh, A., Hazuki, M., Kojima, K., Hirabayashi, J., and Matsumoto, I. (2000) Ligand-binding properties of annexin from Caenorhabditis elegans (annexin XVI, Nex-1). J. Biochem. (Tokyo) 128, 377ā€“381.

    CASĀ  Google ScholarĀ 

  34. Schlecht, U., Nomura, Y., Bachmann, T., and Karube, I. (2002) Reversible surface thiol immobilization of carboxyl group containing haptens to a BIAcore biosensor chip enabling repeated usage of a single sensor surface. Bioconjug. Chem. 13, 188ā€“193s.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  35. Gau, J. J., Lan, E. H., Dunn, B., Ho, C. M., and Woo, J. C. (2001) A MEMS based amperometric detector for E. coli bacteria using self-assembled monolayers. Biosens. Bioelectron. 16, 745ā€“755.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  36. Cooper, M. A., Fiorini, M. T., Abell, C., and Williams, D. H. (2000) Binding of vancomycin group antibiotics to D-alanine and D-lactate presenting self-assembled monolayers. Bioorg. Med. Chem. 8, 2609ā€“2616.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  37. Langmuir, I. (1916) The constitution and fundamental properties of solids and liquids. Part I. Solids. J. Am. Chem. Soc. 38, 2221ā€“2295.

    ArticleĀ  CASĀ  Google ScholarĀ 

  38. Langmuir, I. (1918) The adsorption of gases on plane surfaces of glass, mica and platinium. J. Am. Chem. Soc. 40, 1361ā€“1404.

    ArticleĀ  CASĀ  Google ScholarĀ 

  39. HƤnel, C. and Gauglitz, G. (2002) Comparison of reflectometric interference spectroscopy with other instruments for label-free optical detection. Anal. Bioanal. Chem. 372, 91ā€“100.

    ArticleĀ  PubMedĀ  Google ScholarĀ 

  40. Hengerer, A., Decker, J., Prohaska, E., Hauck, S., Kosslinger, C., and Wolf, H. (1999) Quartz crystal microbalance (QCM) as a device for the screening of phage libraries. Biosens. Bioelectron. 14, 139ā€“144.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  41. Matsuno, H., Niikura, K., and Okahata, Y. (2001) Direct monitoring kinetic studies of DNA polymerase reactions on a DNA-immobilized quartz-crystal microbalance. Chemistry 7, 3305ā€“3312.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

Ā© 2004 Humana Press Inc.

About this protocol

Cite this protocol

Hahnefeld, C., Drewianka, S., Herberg, F.W. (2004). Determination of Kinetic Data Using Surface Plasmon Resonance Biosensors. In: Decler, J., Reischl, U. (eds) Molecular Diagnosis of Infectious Diseases. Methods in Molecular Medicineā„¢, vol 94. Humana Press. https://doi.org/10.1385/1-59259-679-7:299

Download citation

  • DOI: https://doi.org/10.1385/1-59259-679-7:299

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-221-6

  • Online ISBN: 978-1-59259-679-9

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics