Gamma-glutamylcysteine (TFA) is a dipeptide containing a γ-linkage and a thiol-bearing cysteine that enable redox and coordination studies. Researchers explore its role in metal binding, oxidative pathways, and intramolecular hydrogen bonding. The TFA form supports reproducible solubility.
CAT No: R2210
CAS No:283159-88-6
Synonyms/Alias:Gamma-glutamylcysteine (TFA);283159-88-6;Gamma-glutamylcysteine TFA;(2S)-2-amino-5-[[(1R)-1-carboxy-2-sulfanylethyl]amino]-5-oxopentanoic acid;2,2,2-trifluoroacetic acid;L-Cysteine, L-g-glutamyl-, mono(trifluoroacetate) (salt);-glutamylcysteine (TFA);H-gamma-Glu-Cys-OH TFA;AKOS040733224;AT39107;HY-113402A;DA-53482;FG162126;CS-0101974;N5-((R)-1-CARBOXY-2-MERCAPTOETHYL)-L-GLUTAMINE TRIFLUOROACETIC ACID (1:1);(S)-2-Amino-5-(((R)-1-carboxy-2-mercaptoethyl)amino)-5-oxopentanoic acid 2,2,2-trifluoroacetate;N5-((R)-1-Carboxy-2-mercaptoethyl)-L-glutamine compound with 2,2,2-trifluoroacetic acid (1:1);
Gamma-glutamylcysteine (TFA) is a synthetic dipeptide comprising the amino acids L-glutamic acid and L-cysteine, stabilized as its trifluoroacetate salt. As a key intermediate in the biosynthesis of glutathione, one of the most important cellular antioxidants, gamma-glutamylcysteine plays a pivotal role in redox biology and cellular defense mechanisms. Its unique structure, featuring a gamma-peptide bond, imparts distinctive biochemical properties that make it valuable for research into thiol metabolism, oxidative stress responses, and enzymatic pathways involving glutathione synthesis. The compound's relevance extends across biochemistry, molecular biology, and cell biology, where it serves as a critical tool for probing antioxidant networks and sulfur amino acid metabolism.
Glutathione biosynthesis research: Gamma-glutamylcysteine is the immediate biosynthetic precursor to glutathione, formed by the action of gamma-glutamylcysteine synthetase (GCL) and subsequently converted to glutathione via glutathione synthetase. Supplying this dipeptide in experimental systems enables researchers to bypass the rate-limiting step of glutathione synthesis, facilitating studies on glutathione homeostasis, regulation, and turnover. This approach is particularly valuable for investigating cellular responses to oxidative stress, dissecting the regulation of GCL, and elucidating the impact of altered glutathione levels on redox-sensitive signaling pathways.
Redox biology and oxidative stress modeling: The thiol group of gamma-glutamylcysteine confers potent reducing capacity, making it a useful reagent for modeling redox reactions in vitro and in cell-based assays. Researchers employ the compound to manipulate intracellular thiol pools, study the dynamics of disulfide bond formation and reduction, and assess the cellular consequences of altered redox balance. Its application in these contexts provides mechanistic insights into antioxidant defense systems, protein thiol modifications, and the cellular adaptation to oxidative challenges.
Enzymology of glutathione-dependent pathways: As a substrate and intermediate in glutathione metabolism, gamma-glutamylcysteine is instrumental for enzymatic studies involving glutathione synthetase, gamma-glutamyl transpeptidase, and related enzymes. Using this dipeptide, researchers can characterize enzyme kinetics, substrate specificity, and catalytic mechanisms, as well as screen for modulators of glutathione biosynthetic enzymes. These investigations are fundamental for understanding the regulation of glutathione levels and the broader implications for cellular detoxification and metabolic integration.
Analytical method development: The compound is utilized as a reference standard and calibration material in analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its defined structure and chemical stability make it suitable for quantifying gamma-glutamyl dipeptides and related thiol-containing species in biological samples. Accurate measurement of these analytes is essential for biomarker discovery, metabolic profiling, and diagnostic research in redox biology and amino acid metabolism.
Cell culture and biochemical supplementation: In experimental cell culture systems, gamma-glutamylcysteine is used to modulate intracellular glutathione levels and investigate the consequences of enhanced or depleted antioxidant capacity. Supplementation with this dipeptide supports studies on cellular proliferation, viability, and response to environmental stressors, providing a controlled means to dissect the role of glutathione in cellular physiology. Its use in these applications underpins research into mechanisms of cytoprotection, metabolic adaptation, and redox regulation across diverse cell types.
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