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

Xinming Li, Baoxin Zhang, Chaoxian Yan, Jin Li, Song Wang, Xiangxu Wei, Xiaoyan Jiang, Panpan Zhou and Jianguo Fang ()
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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

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-10807-8

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