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Reaction-based fluorogenic probes for selective detection of cysteinyl oxidation in living cells

ABSTRACT: Measuring reactive oxygen, nitrogen and sulfur species in cells is established technology, but turn-on fluorescence tools for detecting the products of their reaction with protein cysteines remain essentially unknown. Toward this goal, here we describe fluorogenic probes for sulfenic acid, a redox modification of protein cysteines inextricably linked to signaling and oxidative stress.

ORGANISM(S): Homo Sapiens

SUBMITTER: Jing Yang

PROVIDER: PXD029176 | iProX | Mon Oct 18 00:00:00 BST 2021

REPOSITORIES: iProX

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Reaction-based fluorogenic probes for detecting protein cysteine oxidation in living cells.

Ferreira Renan B RB Fu Ling L Jung Youngeun Y Yang Jing J Carroll Kate S KS

Nature communications 20220921 1

'Turn-on' fluorescence probes for detecting H2O2 in cells are established, but equivalent tools to monitor the products of its reaction with protein cysteines have not been reported. Here we describe fluorogenic probes for detecting sulfenic acid, a redox modification inextricably linked to H2O2 signaling and oxidative stress. The reagents exhibit excellent cell permeability, rapid reactivity, and high selectivity with minimal cytotoxicity. We develop ...[more]

PMID: 36130931

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Reaction-based fluorogenic probes for detecting protein cysteine oxidation in living cells.

Project description:'Turn-on' fluorescence probes for detecting H2O2 in cells are established, but equivalent tools to monitor the products of its reaction with protein cysteines have not been reported. Here we describe fluorogenic probes for detecting sulfenic acid, a redox modification inextricably linked to H2O2 signaling and oxidative stress. The reagents exhibit excellent cell permeability, rapid reactivity, and high selectivity with minimal cytotoxicity. We develop a high-throughput assay for measuring S-sulfenation in cells and use it to screen a curated kinase inhibitor library. We reveal a positive association between S-sulfenation and inhibition of TK, AGC, and CMGC kinase group members including GSK3, a promising target for neurological disorders. Proteomic mapping of GSK3 inhibitor-treated cells shows that S-sulfenation sites localize to the regulatory cysteines of antioxidant enzymes. Our studies highlight the ability of kinase inhibitors to modulate the cysteine sulfenome and should find broad application in the rapidly growing field of redox medicine.

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Author Correction: Reaction-based fluorogenic probes for detecting protein cysteine oxidation in living cells.

Project description: Not available

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