Dehydroglutathione, a glutathione derivative to introduce non-reversible glutathionylation.

ABSTRACT: Protein cysteine is susceptible to diverse oxidations, including disulfide, S-sulfenylation, S-nitrosylation, and S-glutathionylation, that regulate many biological processes in physiology and diseases. Despite evidence supporting distinct biological outcomes of individual cysteine oxoforms, the approach for examining functional effects resulting from a specific cysteine oxoform, such as S-glutathionylation, remains limited. In this report, we devised a dehydroglutathione (dhG)-mediated strategy, named G-PROV, that introduces a non-reducible glutathionylation mimic to the protein with the subsequent delivery of the modified protein to cells to examine the "phenotype" attributed to "glutathionylation". We applied our strategy to fatty acid binding protein 5 (FABP

SUBMITTER: Oppong D 

PROVIDER: S-EPMC12143294 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature