7729-20-6

Basic information

• Product Name: (H-CYS-GLY-OH)2
• Synonyms: CYS-GLY, OXIDIZED ACETATE SALT;CYS[CYS-GLY]-GLY;L-CYSTINYL-BIS-GLYCINE;(H-CYS-GLY-OH)2;(H-Cys-Gly-OH)2 (Disulfide bond);CYS-GLY, OXIDIZED ACETATE;Cys-Gly, oxidised, acetate salt;Cys-Gly, oxidized
• CAS NO: 7729-20-6
• Molecular Formula: C₁₀H₁₈N₄O₆S₂
• Molecular Weight: 354.4
• Mol File: 7729-20-6.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 788.5°Cat760mmHg
• Flash Point: 430.7°C
• Appearance: /
• Density: 1.535g/cm³
• Vapor Pressure: 2.85E-27mmHg at 25°C
• Refractive Index: 1.626
• Storage Temp.: −20°C
• PKA: 2.72±0.10(Predicted)
• CAS DataBase Reference: (H-CYS-GLY-OH)2(CAS DataBase Reference)
• NIST Chemistry Reference: (H-CYS-GLY-OH)2(7729-20-6)
• EPA Substance Registry System: (H-CYS-GLY-OH)2(7729-20-6)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 7729-20-6(Hazardous Substances Data)

Usage

Description

Cystinyl-bis-glycine is a dipeptide intermediate in the synthesis of oxidized glutathione that is composed of two cysteinylglycine peptides linked by a disulfide bond. It is formed via nonenzymatic oxidation of cysteinylglycine, a glutathione catabolite produced by γ-glutamyl transpeptidase.

Definition

ChEBI: An organic disulfide obtained by the oxidation of two Cys-Gly molecules which are then linked via a disulfide bond.

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 
• 70-18-8 GLUTATHIONE 
• 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 
• 100232-14-2 N-Carbobenzoxy-S-(4-methoxy-benzyl)-L-cysteinyl-glycin 
• 13492-61-0 N,N'-[N,N'-bis-(4-nitro-benzyloxycarbonyl)-L-cystyl]-bis-glycine diethyl ester 
• 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 
• 27025-41-8 Oxidized glutathione 
• 92034-35-0 S-(4-Methoxy-benzyl)-L-cysteinyl-glycin 
• 26988-56-7 S-Diphenylmethyl-L-cysteinylglycin 
• 33628-67-0 Benzyloxycarbonyl-cystyl-glycin-piperonylester 
• 121475-41-0 N,N'-[N,N'-bis-(4-nitro-benzyloxycarbonyl)-L-cystyl]-bis-glycine 

Downstream Products

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

Relevant articles and documents

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

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