Surface Plasmon Resonance

Abstract

Surface plasmon resonance is an optical resonance effect where the backside of a thin conductive mirror affects the angle at which there is a minimum of reflected light.

Keywords: surface plasmon resonance; binding reaction; biosensor; optical biosensor; real‐time biosensor; sensor

Figure 1.

Schematic diagram of some of the important components of an SPR detector system. The blue area on the backside of the thin gold mirror is the active area where changes in the dielectric constant change the angle of the dark band in the reflected light. The light source (monochromatic) is directed through a prism to a detector (here represented by an eye) where changes in the dielectric constant are recorded. For example, when proteins bind to ligands attached (through a linker) to the gold surface, a change in dielectric constant occurs which is correlated with SPR change.

Figure 2.

A binding signal (here ETS‐1 DBD (part of an oncogene) and a peptide RV (a domain of the associated protein)) shows initial binding followed by a stochastic steady state (loosely, an equilibrium) from a Biacore instrument. When the flow of peptide/analyte (RV) is replaced with a flow of buffer, this reversible binding reaction relaxes towards a zero‐bound complex concentration, as shown by reduction in the SPR signal. The signal is measured in response units (RU). Each RU represents about 1/3000th of a degree.

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References

Karlsson R and Fält A (1997) Experimental design for kinetic analysis of protein–protein interactions with surface plasmon resonance biosensors. Journal of Immunological Methods 200: 121–133.

Langmuir I (1918) The adsorption of gases on plane surfaces of glass, mica and platinum. Journal of the American Chemical Society 40: 1361.

Lopez R, Haynes TE, Boatner LA, Feldman LC and Haglund RF Jr (2002) Temperature‐controlled surface plasmon resonance in VO 2 nanorods. Optics Letters 27(15): 1327–1329.

Welford K (1991) Surface plasmon–polaritons and their uses. Optical and Quantum Electronics 23: 1–27.

Further Reading

Fisher RJ, Fivash M, Casas‐Finet J et al. (1994) Real‐time BIAcore measurements of Escherichia coli single‐stranded DNA binding (SSB) protein to polydeoxythymidylic acid reveal single‐state kinetics with steric cooperativity. Methods: A Companion to Methods in Enzymology 6: 121–133. [This paper details methods for developing kinetic models of more complex binding systems.].

Fivash M, Towler EM and Fisher RJ (1998) BIAcore for macromolecular interaction. Current Opinion in Biotechnology 9(1): 97–101. [This review details the growth and use of SPR technology.].

Karlsson R and Fält A (1997) Experimental design for kinetic analysis of protein–protein interactions with surface plasmon resonance biosensors. Journal of Immunological Methods 200: 121–133.

Myszka DG, Morton TA, Doyle ML and Chaiken IM (1997) Kinetic analysis of protein antigen–antibody interaction limited by mass transport on an optical biosensor. Biophysical Chemistry 64: 127–137. [This paper examines the issues of transport with flow systems like the Biacore instrument, and shows that a simple model for this effect is usually adequate.].

Rich RL and Myszka DG (2001) Survey of the year 2000 commercial optical biosensor literature. Journal of Molecular Recognition 14(5): 273–294.

Websites. http://www.biacore.com/ http://www.cores.utah.edu/interaction/ http://www.med.unc.edu/wrkunits/2depts/biochem/MACINFAC/biacore.html

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How to Cite close
Fivash, Matthew J(Sep 2005) Surface Plasmon Resonance. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0003861]