Surface plasmon resonance is an optical technique utilized for detecting molecular interactions. Binding of a mobile molecule (analyte) to a molecule immobilized on a thin metal film (ligand) changes the refractive index of the film. The angle of extinction of light, reflected after polarized light impinges upon the film, is altered, monitored as a change in detector position for the dip in reflected intensity (the surface plasmon resonance phenomenon). Because the method strictly detects mass, there is no need to label the interacting components, thus eliminating possible changes of their molecular properties. We have utilized surface plasmon resonance to study the interaction of proteins of hair cells.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsSpringer Nature is developing a new tool to find and evaluate Protocols. Learn more
References
Schuck, P. (1997) Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Struct. 26, 541–566.
Ramakrishnan, N. A., Drescher, M. J., Sheikhali, S. A., Khan, K. M., Hatfield, J. S., Dickson, M. J., and Drescher, D. G. (2006) Molecular identification of an N-type Ca2+ channel in saccular hair cells. Neuroscience 139, 1417–1434.
Kretschmann, E. and Raether, H. (1968) Radiative decay of non-radiative surface plasmons excited by light. Z. Naturforsch. Teil. A. 23, 2135–2136.
Karlsson, R., Roos, H., Fögerstam, L., and Persson, B. (1994) Kinetic and concentration analysis using BIA technology. Methods: Companion Methods Enzymol. 6, 99–110.
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. 143,513–526.
Johnsson, B., Lofas, S., and Lindquist, G. (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198, 268–277.
Steffner P. and Markey F. (1997) When the chips are down. BIA J. 1, 11–15.
Myszka, D. G., He, X., Dembo, M., Morton, T. A., and Goldstein B. (1998) Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data. Biophys. J. 75, 583–594.
BIACORE. (1998). BIAevaluation Version 3 Software Handbook. Chapter 5. Evaluating concentration data. 5.1–5.10.
Acknowledgments
This work was supported by NIH R01 DC000156, NIH R01 DC004076, and the American Hearing Research Foundation. We thank Dr. Stanley Terlecky, Department of Pharmacology, Wayne State University, for use of the Bia coore 3000 instrument.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Humana Press, a part of Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Drescher, D.G., Drescher, M.J., Ramakrishnan, N.A. (2009). Surface Plasmon Resonance (SPR) Analysis of Binding Interactions of Proteins in Inner-Ear Sensory Epithelia. In: Sokolowski, B. (eds) Auditory and Vestibular Research. Methods in Molecular Biology™, vol 493. Humana Press. https://doi.org/10.1007/978-1-59745-523-7_20
Download citation
DOI: https://doi.org/10.1007/978-1-59745-523-7_20
Publisher Name: Humana Press
Print ISBN: 978-1-934115-62-6
Online ISBN: 978-1-59745-523-7
eBook Packages: Springer Protocols