The BRET technology and its application to screening assays

被引：112

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.

引用

页码：311 / 324

页数：13

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