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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.

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The BRET technology and its application to screening assays

Bacart

Corbel

Jockers

et al. 2008

Biotechnology Journal

146

138

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An ELISA for quantification of recombinant human EGF in production process samples, serum and urine

et al. 2018

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Impact of Receptor Downregulation on Clearance of Two Human EGFs With Different Receptor Binding Activity

Sizemore¹,

Wright²,

Mueller³

et al. 1996

Peptides

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Abstract: Two sensitive ELISA methods have been validated for quantitation of hEGF1-53 and hEGF1-48 in rat plasma. Their utility has been demonstrated in the application of assaying immunoreactive concentration of exogenous and endogenous epidermal growth factors.

Cited by 9 publications

References 22 publications

The BRET technology and its application to screening assays

The BRET technology and its application to screening assays

An ELISA for quantification of recombinant human EGF in production process samples, serum and urine

Impact of Receptor Downregulation on Clearance of Two Human EGFs With Different Receptor Binding Activity

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