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Luciferase-induced photoreductive uncaging of small-molecule effectors

Published inNature Communications, vol. 9, no. 3539
Publication date2018
Abstract

Bioluminescence resonance energy transfer (BRET) is extensively used to study dynamic systems and has been utilized in sensors for studying protein proximity, metabolites, and drug concentrations. Herein, we demonstrate that BRET can activate a ruthenium-based photocatalyst which performs bioorthogonal reactions. BRET from luciferase to the ruthenium photocatalyst is used to uncage effector molecules with up to 64 turnovers of the catalyst, achieving concentrations >0.6 μM effector with 10 nM luciferase construct. Using a BRET sensor, we further demonstrate that the catalysis can be modulated in response to an analyte, analogous to allosterically controlled enzymes. The BRET-induced reaction is used to uncage small-molecule drugs (ibrutinib and duocarmycin) at biologically effective concentrations in cellulo.

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Citation (ISO format)
LINDBERG, Eric et al. Luciferase-induced photoreductive uncaging of small-molecule effectors. In: Nature Communications, 2018, vol. 9, n° 3539. doi: 10.1038/s41467-018-05916-9
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ISSN of the journal2041-1723
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Creation09/24/2018 9:51:00 AM
First validation09/24/2018 9:51:00 AM
Update time03/15/2023 8:41:46 AM
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