Luciferase‐Induced Photouncaging: Bioluminolysis

Bioluminescence resonance energy transfer (BRET) has been widely used for studying dynamic processes in biological systems such as protein–protein interactions and other signaling events. Aside from acting as a reporter, BRET can also turn on functions in living systems. Herein, we report the applic...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2019-11, Vol.58 (45), p.16033-16037
Main Authors: Chang, Dalu, Lindberg, Eric, Feng, Suihan, Angerani, Simona, Riezman, Howard, Winssinger, Nicolas
Format: Article
Language:English
Subjects:
Biological activity
Bioluminescence
BRET
Cells (biology)
Coumarin
Coumarins - metabolism
Energy transfer
Enzyme inhibitors
Fluorescence Resonance Energy Transfer - methods
halotag
HeLa Cells
Humans
Kinases
Light sources
luciferase
Luciferases - metabolism
Luminescent Measurements - methods
Luminescent Proteins - metabolism
optochemical reactions
Protein Binding
Protein interaction
Proteins
Pyrazoles - metabolism
Pyrimidines - metabolism
Reaction kinetics
Substrates
uncaging reactions
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Summary:Bioluminescence resonance energy transfer (BRET) has been widely used for studying dynamic processes in biological systems such as protein–protein interactions and other signaling events. Aside from acting as a reporter, BRET can also turn on functions in living systems. Herein, we report the application of BRET to performing a biorthogonal reaction in living cells; namely, releasing functional molecules through energy transfer to a coumarin molecule, a process termed bioluminolysis. An efficient BRET from Nanoluc‐Halotag chimera protein (H‐Luc) to a coumarin substrate yields the excited state of coumarin, which in turn triggers hydrolysis to uncage a target molecule. Compared to the conventional methods, this novel uncaging system requires no external light source and shows fast kinetics (t1/2
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201907734