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A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage

Author

Listed:
  • Xinming Li

    (Lanzhou University)

  • Baoxin Zhang

    (Lanzhou University)

  • Chaoxian Yan

    (Lanzhou University)

  • Jin Li

    (Lanzhou University)

  • Song Wang

    (Lanzhou University)

  • Xiangxu Wei

    (Lanzhou University)

  • Xiaoyan Jiang

    (Lanzhou University)

  • Panpan Zhou

    (Lanzhou University)

  • Jianguo Fang

    (Lanzhou University)

Abstract

Small molecule probes are indispensable tools to explore diverse cellular events. However, finding a specific probe of a target remains a high challenge. Here we report the discovery of Fast-TRFS, a specific and superfast fluorogenic probe of mammalian thioredoxin reductase, a ubiquitous enzyme involved in regulation of diverse cellular redox signaling pathways. By systematically examining the processes of fluorophore release and reduction of cyclic disulfides/diselenides by the enzyme, structural factors that determine the response rate and specificity of the probe are disclosed. Mechanistic studies reveal that the fluorescence signal is switched on by a simple reduction of the disulfide bond within the probe, which is in stark contrast to the sensing mechanism of published probes. The favorable properties of Fast-TRFS enable development of a high-throughput screening assay to discover inhibitors of thioredoxin reductase by using crude tissue extracts as a source of the enzyme.

Suggested Citation

  • Xinming Li & Baoxin Zhang & Chaoxian Yan & Jin Li & Song Wang & Xiangxu Wei & Xiaoyan Jiang & Panpan Zhou & Jianguo Fang, 2019. "A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10807-8
    DOI: 10.1038/s41467-019-10807-8
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