The BRET technology and its application to screening assays.
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.
Bacart
Johan
J
UMR 8090, CNRS, Université Lille 2, Lille, France.
Corbel
Caroline
C
Jockers
Ralf
R
Bach
Stéphane
S
Couturier
Cyril
C
D001681:Biological Assay / Q000639:trends*; D015195:Drug Design; D031541:Fluorescence Resonance Energy Transfer / Q000639:trends*; D008163:Luminescent Measurements / Q000639:trends*; D008164:Luminescent Proteins; D025941:Protein Interaction Mapping / Q000379:methods*
D008164:Luminescent Proteins