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Luciferase-induced photoreductive uncaging of small-molecule effectors

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  • Eric Lindberg

    (University of Geneva)

  • Simona Angerani

    (University of Geneva)

  • Marcello Anzola

    (University of Geneva)

  • Nicolas Winssinger

    (University of Geneva)

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.

Suggested Citation

  • Eric Lindberg & Simona Angerani & Marcello Anzola & Nicolas Winssinger, 2018. "Luciferase-induced photoreductive uncaging of small-molecule effectors," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05916-9
    DOI: 10.1038/s41467-018-05916-9
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