Dataset Information

Dehydroglutathione to induce glutathione modification in protein

ABSTRACT: Protein S-glutathionylation is one of the major cysteine oxidations regulating redox signaling and oxidative stress. In this study, we developed a glutathione-derived chemical tool, namely dehydroglutathione, that can introduce a non-reducible glutathionylation mimic to protein, which can be utilized for analyzing the functional effects of glutathionylation. Dehydroglutathione reacts with protein cysteines to form a thio-ether based glutathione modification in proteins. We applied dehydroglutathione to fatty acid binding protein 5 (FABP5). Dehydroglutathione modification in FABP5 was analyzed by LC-MS/MS to identify the cysteine sites of modification.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Young-Hoon Ahn

LAB HEAD: Young-Hoon Ahn

PROVIDER: PXD061319 | Pride | 2025-07-14

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	FABP5_dhG_MSMS_Eclipse.raw	Raw
	checksum.txt	Txt
	msms.txt	Txt
	uniprotkb_proteome_UP000005640_AND_revi_2024_10_05.fasta	Fasta

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Publications

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

Oppong Daniel D Padmavathi Rayavarapu R Kukulage Dhanushika S K DSK Shivamadhu Madhu C MC Newberry Elizabeth A EA Faustino Anneliese M AM Tang Hsin-Yao HY Ahn Young-Hoon YH

RSC chemical biology 20250521 7

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 dehydroglutath ...[more]

PMID: 40487857

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