Surface Plasmon Resonance
Interactions between macromolecules play a central role in most biological processes. Their analysis in vitro can shed light on their role in the intact cell by providing valuable information on specificity, affinity, and structure-function relationships. Significant progress in this respect has come with the advent, in the last few years, of commercially available biosensor technology (1). This has allowed the study of macromolecular interactions in real time, providing a wealth of high-quality binding data that can be used for kinetic analysis, affinity measurements, competition studies, and so on. A major advantage of biosensor analysis is that there is no requirement for labeling one of the interacting components and then separating bound from free molecules—a fact that simplifies experimental procedures and provides more accurate measurements.
KeywordsSurface Plasmon Resonance Resonance Unit Dissociation Rate Constant Immobilize Ligand Biosensor Technology
- 5.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. Biosensors 2, 291–336.Google Scholar
- 7.Zhou, M., Felder, S., Rubinstein, M., Hurwitz, D. R., Ullrich, A., Lax, I., and Schlessinger, J. (1993) Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerisation model for receptor activation. Biochemistry 32, 8193–8198.PubMedCrossRefGoogle Scholar
- 8.Panayotou, G., Gish, G., End, P., Truong, O., Gout, I., Dhand, R., Fry, M. J., Hiles, I., Pawson, T., and Waterfield, M. D. (1993) Interactions between SH2 domains and tyrosine-phosphorylated PDGF β-receptor sequences: analysis of kinetic parameters using a novel biosensor-based approach. Mol. Cell. Biol. 13, 3567–3576.PubMedGoogle Scholar