7729-20-6

Usage

Uses

Used in Pharmaceutical Industry:
(H-CYS-GLY-OH)2 is used as an intermediate in the synthesis of oxidized glutathione for its antioxidant and detoxification properties. It plays a crucial role in maintaining cellular redox balance and protecting cells from oxidative stress and damage.
Used in Cosmetic Industry:
(H-CYS-GLY-OH)2 is used as an active ingredient in cosmetic products for its skin-whitening and anti-aging effects. It inhibits melanin synthesis and promotes collagen production, resulting in a brighter and more youthful appearance.
Used in Food Industry:
(H-CYS-GLY-OH)2 is used as a functional ingredient in food products for its antioxidant properties. It helps to protect food products from oxidation and extend their shelf life.
Used in Research Applications:
(H-CYS-GLY-OH)2 is used as a research tool in studying the role of glutathione in various biological processes, including redox regulation, detoxification, and cell signaling. It aids in understanding the mechanisms of oxidative stress and its impact on health and disease.

InChI:InChI=1/C10H18N4O6S2/c11-5(9(19)13-1-7(15)16)3-21-22-4-6(12)10(20)14-2-8(17)18/h5-6H,1-4,11-12H2,(H,13,19)(H,14,20)(H,15,16)(H,17,18)

Upstream product

• 33642-58-9 N,N'-L-cystyl-bis-glycine diethyl ester 
• 19246-18-5 cysteinylglycine 
• 26988-56-7 S-Diphenylmethyl-L-cysteinylglycin 
• 27025-41-8 Oxidized glutathione 
• 70-18-8 GLUTATHIONE 
• 13492-61-0 N,N'-[N,N'-bis-(4-nitro-benzyloxycarbonyl)-L-cystyl]-bis-glycine diethyl ester 
• 100232-14-2 N-Carbobenzoxy-S-(4-methoxy-benzyl)-L-cysteinyl-glycin 
• 30040-93-8 (6R,11R)-methyl 11-((tert-butoxycarbonyl)amino)-6-((2-methoxy-2-oxoethyl)carbamoyl)-2,2-dimethyl-4,12-dioxo-3-oxa-8,9-dithia-5,13-diazapentadecan-15-oate 
• 101035-11-4 N-Carbobenzoxy-S-(4-methoxy-benzyl)-L-cysteinyl-glycin-ethylester 
• 95107-90-7 N,N'-di-p-nitrocarbobenzoxy-L-cystine 
• 51507-96-1 L-cystine N-carboxy anhydride 
• 6968-11-2 N,N'-bis(benzyloxycarbonyl)-L-cystine 
• 92034-35-0 S-(4-Methoxy-benzyl)-L-cysteinyl-glycin 
• 33628-67-0 Benzyloxycarbonyl-cystyl-glycin-piperonylester 

Downstream Products

• 7669-84-3 S-benzyl-L-cysteinylglycine 
• 7783-06-4 hydrogen sulfide 
• 7664-41-7 ammonia 
• 127-17-3 2-oxo-propionic acid 

Relevant academic research and scientific papers

Charge Transfer in Peptides. Effects of Temperature, Peptide Length and Solvent Conditions upon Intramolecular One-electron Reactions Involving Tryptophan and Tyrosine

Tryptophyl-tyrosyl peptides, TrpH-(Gly)n-TyrOH and cyclic c-TrpH-TyrOH, were oxidised selectively at the indole group with electron accepting radicals (N.3 or Br.-2) in aqueous solution, using pulse r

Carnosine dipeptidase II (CNDP2) protects cells under cysteine insufficiency by hydrolyzing glutathione-related peptides

The knockout (KO) of the cystine transporter xCT causes ferroptosis, a type of iron-dependent necrotic cell death, in mouse embryonic fibroblasts, but this does not occur in macrophages. In this study, we explored the gene that supports cell survival under a xCT deficiency using a proteomics approach. Analysis of macrophage-derived peptides that were tagged with iTRAQ by liquid chromatography-mass spectrometry revealed a robust elevation in the levels of carnosine dipeptidase II (CNDP2) in xCT KO macrophages. The elevation in the CNDP2 protein levels was confirmed by immunoblot analyses and this elevation was accompanied by an increase in hydrolytic activity towards cysteinylglycine, the intermediate degradation product of glutathione after the removal of the γ-glutamyl group, in xCT KO macrophages. Supplementation of the cystine-free media of Hepa1-6 cells with glutathione or cysteinylglycine extended their survival, whereas the inclusion of bestatin, an inhibitor of CNDP2, counteracted the effects of these compounds. We established CNDP2 KO mice by means of the CRISPR/Cas9 system and found a decrease in dipeptidase activity in the liver, kidney, and brain. An acetaminophen overdose (350 mg/kg) showed not only aggravated hepatic damage but also renal injury in the CNDP2 KO mice, which was not evident in the wild-type mice that were receiving the same dose. The aggravated renal damage in the CNDP2 KO mice was consistent with the presence of abundant levels of CNDP2 in the kidney, the organ prone to developing ferroptosis. These collective data imply that cytosolic CNDP2, in conjugation with the removal of the γ-glutamyl group, recruits Cys from extracellular GSH and supports redox homeostasis of cells, particularly in epithelial cells of proximal tubules that are continuously exposed to oxidative insult from metabolic wastes that are produced in the body.

A study of the glutathione metaboloma peptides by energy-resolved mass spectrometry as a tool to investigate into the interference of toxic heavy metals with their metabolic processes

To better understand the fragmentation processes of the metal-biothiol conjugates and their possible significance in biological terms, an energy-resolved mass spectrometric study of the glutathione conjugates of heavy metals, of several thiols and disulfides of the glutathione metaboloma has been carried out. The main fragmentation process of γ-glutamyl compounds, whether in the thiol, disulfide, thioether or metal-bis-thiolate form, is the loss of the γ-glutamyl residue, a process which ERMS data showed to be hardly influenced by the sulfur substitution. However, loss of the γ-glutamyl residue from the mono-S-glutathionyl-mercury (II) cation is a much more energetic process, possibly pointing at a strong coordination of the carboxylic group to the metal. Moreover, loss of neutral mercury from ions containing the γ-glutamyl residue to yield a sulfenium cation was a much more energetic process than those not containing them, suggesting that the redox potential of the thiol/disulfide system plays a role in the formal reduction of the mercury dication in the gas phase. Occurrence of complementary sulfenium and protonated thiol fragments in the spectra of protonated disulfides of the glutathione metaboloma mirrors the thiol/disulfide redox process of biological importance. The intensity ratio of the fragments is proportional to the reduction potential in solution of the corresponding redox pairs. This finding has allowed the calculation of the previously unreported reduction potentials for the disulfide/thiol pair of cysteinylglycine, thereby confirming the decomposition scheme of bis- and mono-S-glutathionyl-mercury (II) ions. Finally, on the sole basis of the mass spectrometric fragmentation of the glutathione-mercury conjugates, and supported by independent literature evidence, an unprecedented mechanism for mercury ion-induced cellular oxidative stress could be proposed, based on the depletion of the glutathione pool by a catalytic mechanism acting on the metal (II)-thiol conjugates and involving as a necessary step the enzymatic removal of the glutamic acid residue to yield a mercury (II)-cysteinyl-glycine conjugate capable of regenerating neutral mercury through the oxidation of glutathione thiols to the corresponding disulfides. Copyright

Reactivite du nitrite de sodium. V. Action sur les amino-acides, peptides et proteines

The action of sodium nitrite on various amino-acids was re-examined in conditions approximating to a biological medium. 13C-NMR provides evidence of the existence of intramolecular ring closures and the formation of 5-membered rings with ornithine, citrulline and arginine.The reaction of cystine shows the opening of the sulphur bridges, whereas cysteine leads to the formation of carboxy-thiiran and 3-sulpho-lactic acid.The hydrolysis of the amide bonds of asparagine and glutamine is complete whereas the peptides studied - carnosine and aspartam - do not undergo hydrolysis of the peptide linkage.However, the first deamination of glutathion (γ-Glu-Cys-Gly) induces the peptide link to be broken and a cyclization with the formation of lactone to occur.A second deamination takes place on the cysteinyl residue released and allows the formation of a thiiran by intramolecular cyclization with the thiol group.The formation of thiiran was also observed with oxidized glutathion which has an S-S bridge.Finally, the formation of nitrosamines was detected by 15N-NMR during the reaction of sodium nitrite with two commercial products available to the general public.