The BRET technology and its application to screening assays

被引:114
作者
UMR 8090, CNRS, Université Lille 2, 1 rue du Professeur Calmette, 59019 Lille Cedex, France [1 ]
不详 [2 ]
不详 [3 ]
不详 [4 ]
机构
[1] UMR 8090, CNRS, Université Lille 2, 59019 Lille Cedex
[2] CNRS UPS 2682, Protein Phosphorylation and Disease Laboratory, Station Biologique, Roscoff
[3] Institut Cochin, Université Paris Descartes, CNRS UMR 8104, Paris
[4] Inserm U567, Paris
来源
Biotechnol. J. | 2008年 / 3卷 / 311-324期
关键词
Bioluminescence resonance energy transfer; Drug discovery; High throughput screening assays; Protein-protein interaction;
D O I
10.1002/biot.200700222
中图分类号
学科分类号
摘要
The bioluminescence resonance energy transfer (BRET) method is based on resonance energy transfer between a light-emitting enzyme and a fluorescent acceptor. Since its first description in 1999, several versions of BRET have been described using different substrates and energy donor/acceptor couples. Today, BRET is considered as one of the most versatile techniques for studying the dynamics of protein-protein interactions in living cells. Various studies have applied BRET-based assays to screen new receptor ligands and inhibitors of disease-related-proteases. Inhibitors of protein-protein interactions are likely to become a new major class of therapeutic drugs, and BRET technology is expected to play an important role in the identification of such compounds. This review describes the original BRET-based methodology, more recent variants, and potential applications to drug screening. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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页码:311 / 324
页数:13
相关论文
共 135 条
[21]  
Ramsay D., Kellett E., McVey M., Rees S., Milligan G., Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences, Biochem. J, 365, pp. 429-440, (2002)
[22]  
Subramanian C., Xu Y., Johnson C.H., von Arnim A.G., In vivo detection of protein-protein interaction in plant cells using BRET, Methods Mol. Biol, 284, pp. 271-286, (2004)
[23]  
Gehret A.U., Bajaj A., Naider F., Dumont M.E., Oligomerization of the yeast alpha-factor receptor: Implications for dominant negative effects of mutant receptors, J. Biol. Chem, 281, pp. 20698-20714, (2006)
[24]  
Wu P., Brand L., Resonance energy transfer: Methods and applications, Anal. Biochem, 218, pp. 1-13, (1994)
[25]  
Haugland R.P., Yguerabide J., Stryer L., Dependence of the kinetics of singlet-singlet energy transfer on spectral overlap, Proc. Natl. Acad. Sci. USA, 63, pp. 23-30, (1969)
[26]  
Keller R.C., Silvius J.R., De Kruijff B., Characterization of the resonance energy transfer couple coumarin-BODIPY and its possible applications in protein-lipid research, Biochem. Biophys. Res. Commun, 207, pp. 508-514, (1995)
[27]  
Charest P.G., Terrillon S., Bouvier M., Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET, EMBO Rep, 6, pp. 334-340, (2005)
[28]  
Jiang L.I., Collins J., Davis R., Lin K.M., Et al., Use of a cAMP BRET sensor to characterize a novel regulation of cAMP by the sphingosine 1-phosphate/G13 pathway, J. Biol. Chem, 282, pp. 10576-10584, (2007)
[29]  
Kasprzak A.A., The use of FRET in the analysis of motor protein structure, Methods Mol. Biol, 392, pp. 183-197, (2007)
[30]  
Clegg R.M., Murchie A.I., Zechel A., Lilley D.M., Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer, Proc. Natl. Acad. Sci. USA, 90, pp. 2994-2998, (1993)