Abstract
Surface plasmon resonance (SPR) is a novel biophysical detection method. In combination with sophisticated surface chemistries and sensing instrumentations, SPR biosensors are approved as tools for molecular interaction studies. SPR plays also a role in interaction proteomics. Once being detected in urine, SPR helps to unravel the functions of new proteins. Due to its outstanding analytical characteristics, SPR also moves more and more into the realm of quantitative analyses in the clinical laboratory. Complex urine determinations of proteins and/or metabolites will bring the SPR biosensor both to the core lab and to point-of-care-testing.
This review delineates first the optical phenomena of SPR near to the gold surface, and also the main features of bioconjugation chemistry on a solid-state surface. Then the kinetic calculation of molecular interaction analysis using SPR is introduced. In order to portray the capability of the method, new applications in urine proteomics and proteinuria diagnostics are finally described in detail.
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References
Ekins, R. P. (1999) Immunoassay and other ligand assays: from isotopes to luminescence. J. Clin. Ligand Assay 22, 61–77
Luppa, P. B., Sokoll, L. J., and Chan, D. W. (2001) Immunosensors – Principles and applications to clinical chemistry. Clin. Chim. Acta 314, 1–26
Mullett, W., Lai, E. P., and Yeung, J. M. (2000) Surface plasmon resonance-based immunoassays. Methods 22, 77–91
Pearson, J. E., Gill, A., Vadgama, P. (2000) Analytical aspects of biosensors. Ann. Clin. Biochem. 37, 119–145
Rogers, K. R. (2000) Principles of affinity-based biosensors. Mol. Biotechnol. 14, 109–129
Ng, J. H., Ilag, L. L. (2003) Biochips beyond DNA: technologies and applications. Biotechnol. Annu. Rev. 9, 1–149
Marquette, C. A. and Blum, L. J. (2006) State of the art and recent advances in immunoanalytical systems. Biosens. Bioelectron 21, 1424–1433
Newman, J. D. and Setford, S. J. (2006) Enzymatic biosensors. Mol. Biotechnol. 32, 249–268
Price, C. P., St. John, A., and Hicks, J. M., eds. (2004) Point of Care Testing, 2nd edition. AACC Press, Washington, DC.
Karlsson, R. (2004) SPR for molecular interaction analysis: a review of emerging application areas. J. Mol. Recognit. 17, 151–161
Homola, J., Yee, S, S., and Gauglitz, G. (1999) Surface plasmon resonance sensors: review. Sens. Actuators B Chem. 54, 3–15
Homola, J. (2003) Present and future of surface plasmon resonance biosensors. Anal. Bioanal. Chem. 377, 528–539
Rich, R. L. and Myszka, D. G. (2005) Survey of the year 2003 commercial optical biosensor literature. J. Mol. Recognit. 18, 1–39
Rich, R. L. and Myszka, D. G. (2005) Survey of the year 2004 commercial optical biosensor literature. J. Mol. Recognit. 18, 431–478
Rich, R. L. and Myszka, D. G. (2006) Survey of the year 2005 commercial optical biosensor literature. J. Mol. Recognit. 19, 478–534
Rich, R. L. and Myszka, D. G. (2003) A survey of the year 2002 commercial optical biosensor literature. J. Mol. Recognit. 16, 351–382
Liedberg, B., Nylander, C., and Lundström, I. (1995) Biosensing with surface plasmon resonance – how it all started. Biosens. Bioelectron 10, i–ix
Kyo, M., Usui-Aoki, K., and Koga, H. (2005) Label-free detection of proteins in crude cell lysate with antibody arrays by a surface plasmon resonance imaging technique. Anal. Chem. 77, 7115–7121
Homola, J., Vaisocherová, H., Dostálek, J., and Piliarik, M. (2005) Multi-analyte surface plasmon resonance biosensing. Methods 37, 26–36
Yi, S. J., Yuk, J. S., Jung, S. H., Zhavnerko, G. K., Kim, Y. M., and Ha, K. S. (2003) Investigation of selective protein immobilization on charged protein array by wavelength interrogation-based SPR sensor. Mol. Cells 15, 333–340
Jönsson, U. and Malmqvist, M. (1992) Real time biospecific interaction analysis. The integration of surface plasmon resonance detection, general biospecific interface chemistry and microfluidics into one analytical system. Adv. Biosens. 2, 291–336
Myszka, D. G. (1997) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8, 50–57
Myszka, D. G., Morton, T. A., Doyle, M. L., and Chaiken, I. M. (1997) Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor. Biophys. Chem. 64, 127–137
Khalifa, M. B., Choulier, L., Lortat-Jacob, H., Altschuh, D., and Vernet, T. (2001) Biacore data processing: an evaluation of the global fitting procedure. Anal. Biochem. 293, 194–203
De Crescenzo, G., Pham, P. L., Durocher, Y., and O’Connor-McCourt, M. D. (2003) Transforming growth factor-beta (TGF-β) binding to the extracellular domain of the type II TGF-β receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding. J. Mol. Biol. 328, 1173–1183
Usui-Aoki, K., Shimada, K., Nagano, M., Kawai, M., and Koga, H. (2005) A novel approach to protein expression profiling using antibody microarrays combined with surface plasmon resonance technology. Proteomics 5, 2396–2401
Stenberg, E., Persson, B., Roos, H., and Urbanisczky, C. (1991) Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J. Colloid Interface Sci. 143, 513–526
Lofas, S. and Johnsson, B. (1990) A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands.J. Chem. Soc. Chem. Commun. 21, 1526–1528
Lofas, S. (1995) Dextran modified self-assembled monolayer surfaces for use in biointeraction analysis with surface plasmon resonance. Pure Appl. Chem. 67, 829–834
Ulman, A. (1996) Formation and structure of self-assembled monolayers. Chem. Rev. 96, 1533–1554
Li, X., Wei, X., and Husson, S. M. (2004) Thermodynamic studies on the adsorption of fibronectin adhesion-promoting peptide on nanothin films of poly(2-vinylpyridine) by SPR. Biomacromolecules 5, 869–876
Bilkova, Z., Mazurova, J., Churacek, J., Horak, D., and Turkova, J. (1999) Oriented immobilization of chymotrypsin by use of suitable antibodies coupled to a nonporous solid support. J. Chromatogr. A 852, 141–149
Kindermann, M., George, N., Johnsson, N., and Johnsson, K. (2003) Covalent and selective immobilization of fusion proteins. J. Am. Chem. Soc. 125, 7810–7811
Andersson, K., Hamalainen, M., and Malmqvist, M. (1999) Identification and optimization of regeneration conditions for affinity-based biosensor assays. A multivariate cocktail approach. Anal. Chem. 71, 2475–2481
Karlsson, R., Katsamba, P. S., Nordin, H., Pol, E., and Myszka, D. G. (2006) Analyzing a kinetic titration series using affnity biosensors. Anal. Biochem. 349, 136–147
Metzger, J., Schnitzbauer, A., Meyer, M., Söder, M., Cuilleron, C. Y., and Luppa, P. B. (2003) Binding analysis of 1alpha- and 17alpha-dihydrotestosternone derivatives to homodimeric sex hormone-binding globulin. Biochemistry 42, 13735–13745
McDonnell, J. M. (2001) Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition. Curr Opin Chem Biol. 5, 572–577.
Adachi, J., Kumar, C., Zhang, Y., Olsen, J. V., and Mann, M. (2006) The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biol. 7, R80.1–R80.16
Nedelkov, D., Kiernan, U. A., Niederkofler, E. E., Tubbs, K. A., and Nelson, R. W. (2006) Population proteomics: the concept, attributes, and potential for cancer biomarker research. Mol. Cell Proteomics 5, 1811–1818
Zhukov, A., Schurenberg, M., Jansson, O., Areskoug, D., and Buijs, J. (2004) Integration of surface plasmon resonance with mass spectrometry: automated ligand fishing and sample preparation for MALDI MS using a Biacore 3000 biosensor. J. Biomol. Tech. 15, 112–119
Nedelkov, D. and Nelson, R. W. (2003) Delineating protein-protein interactions via biomolecular interaction analysis-mass spectrometry. J. Mol. Recognit. 16, 9–14
Nedelkov, D. and Nelson, R. W. (2001) Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry. Am. J. Kidney Dis. 38, 481–487
Chung, J. W., Bernhardt, R., and Pyun, J. C. (2006) Sequential analysis of multiple analytes using a surface plasmon resonance (SPR) biosensor. J. Immunol. Methods 311, 178–188
Lung, F. D., Chen, H. Y., and Lin, H. T. (2003) Monitoring bone loss using ELISA and surface plasmon resonance (SPR) technology. Protein Pept. Lett. 10, 313–319
Boozer, C., Kim, G., Cong, S., Guan, H., and Londergan, T. (2006) Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies. Curr. Opin. Biotechnol. 17, 400–405
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Luppa, P.B., Metzger, J., Schneider, H. (2010). Surface Plasmon Resonance Biosensorics in Urine Proteomics. In: Rai, A. (eds) The Urinary Proteome. Methods in Molecular Biology, vol 641. Humana Press. https://doi.org/10.1007/978-1-60761-711-2_12
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DOI: https://doi.org/10.1007/978-1-60761-711-2_12
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