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

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 fa

SUBMITTER: Li X 

PROVIDER: S-EPMC6588570 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature