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Bioluminescence Resonance Energy Transfer
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Bioluminescence Resonance Energy Transfer

Bioluminescence Resonance Energy Transfer (BRET) is a molecular technique that measures protein interactions by transferring energy from a bioluminescent donor to a fluorescent acceptor.

Bioluminescence Resonance Energy Transfer designates a proximity-based detection technique where energy transfer from a bioluminescent donor enzyme to a fluorescent acceptor molecule occurs when they are in close proximity, enabling detection of protein-protein interactions, conformational changes, and molecular proximity in living cells without requiring external excitation light.

The biopharmaceutical industry employs bioluminescence resonance energy transfer assays in drug discovery for screening compounds disrupting or stabilising protein-protein interactions, monitoring receptor conformational changes during ligand binding, tracking intracellular signalling events, and characterising molecular dynamics in living cellular environments. NanoBRET technology using small NanoLuc luciferase donors combined with fluorescent acceptors provides bright signal enabling sensitive detection of cellular interactions. High-throughput screening formats enable compound library evaluation. Cellular target engagement assays using bioluminescence resonance energy transfer confirm that drug candidates reach and bind their intended targets in living cells, providing physiologically relevant binding evidence. As the technique gains wider adoption, bioluminescence resonance energy transfer continues expanding applications in target validation and mechanism studies.

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