6968-11-2

Basic information

• Product Name: N,N'-Bis(benzyloxycarbonyl)-L-cystine
• Synonyms: (CBZ-CYS-OH)2;DI-CBZ-L-CYST;DI-CBZ-L-CYSTINE;DI-N-CBZ-L-CYSTINE;DI-N-BENZYLOXYCARBONYL-L-CYSTINE;(DI-Z-CYS-OH)2;DI-Z-L-CYSTINE;N-ALPHA-N-ALPHA-BIS-Z-L-CYSTINE
• CAS NO: 6968-11-2
• Molecular Formula: C₂₂H₂₄N₂O₈S₂
• Molecular Weight: 508.56
• EINECS: 230-181-3
• Product Categories: Amino Acid Derivatives;Cysteine [Cys, C];Z-Amino Acids and Derivatives;Amino Acids and Derivatives;Amino Acids;Amino Acids (N-Protected);Biochemistry;Cbz-Amino Acids;Z-Amino acid series
• Mol File: 6968-11-2.mol

Chemical Properties

• Melting Point: 118-122 °C (dec.)
• Boiling Point: 766.1 °C at 760 mmHg
• Flash Point: 417.1 °C
• Appearance: White/Powder
• Density: 1.422 g/cm³
• Vapor Pressure: 1.11E-24mmHg at 25°C
• Refractive Index: -91 ° (C=8.8, AcOH)
• Storage Temp.: Store at RT.
• Solubility: almost transparency in Methanol
• PKA: 3.15±0.10(Predicted)
• CAS DataBase Reference: N,N'-Bis(benzyloxycarbonyl)-L-cystine(CAS DataBase Reference)
• NIST Chemistry Reference: N,N'-Bis(benzyloxycarbonyl)-L-cystine(6968-11-2)
• EPA Substance Registry System: N,N'-Bis(benzyloxycarbonyl)-L-cystine(6968-11-2)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• Hazardous Substances Data: 6968-11-2(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Uses

N,N''-Dibenzyloxycarbonyl-L-cystine

InChI:InChI=1/C22H24N2O8S2/c25-19(26)17(23-21(29)31-11-15-7-3-1-4-8-15)13-33-34-14-18(20(27)28)24-22(30)32-12-16-9-5-2-6-10-16/h1-10,17-18H,11-14H2,(H,23,29)(H,24,30)(H,25,26)(H,27,28)/t17-,18-/m0/s1

Upstream product

• 56-89-3 L-cystine 
• 501-53-1 benzyl chloroformate 
• 96289-13-3 N-benzyloxycarbonyl-L-cysteine 
• 91285-94-8 O-benzyl S-(pyridin-2-yl)carbonothioate 
• 96452-48-1 benzyl pyridin-2-yl carbonate 
• 26311-04-6 N-benzyloxycarbonyl-S-trityl-L-cysteine 
• 100-51-6 benzyl alcohol 
• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 928-90-5 5-hexyl-1-ol 
• 2450-71-7 Propargylamine 

Downstream Products

• 2790-86-5 (Z-DL-Cys-GlyOH)2 
• 339175-21-2 (Z-DL-Cys-L-SerOH)2 
• 96289-13-3 N-benzyloxycarbonyl-L-cysteine 
• 2790-85-4 bis-N-carbobenzyloxycysteinyl-bis-glycine diethyl ester 
• 103153-83-9 L-cystine-dianilide 
• 40470-28-8 N.N'-bis-benzyloxycarbonyl-L-cystyl dichloride 
• 104098-35-3 N,N'-bis-benzyloxycarbonyl-L-cystine bis-(2-hydroxy-ethylamide) 
• 116973-09-2 N,N'-bis-benzyloxycarbonyl-L-cystine di-p-toluidide 
• 103401-69-0 N,N'-bis-benzyloxycarbonyl-L-cystine bis-(N'-benzoyl-hydrazide) 
• 104511-01-5 N,N'-bis-benzyloxycarbonyl-L-cystine di-p-anisidide 
• 116151-93-0 N,N'-bis-benzyloxycarbonyl-L-cystine bis-[N'-(4-nitro-benzoyl)-hydrazide] 
• 103331-42-6 N,N'-bis-benzyloxycarbonyl-L-cystine-bis-(N'-isonicotinoyl-hydrazide) 
• 6304-83-2 monobenzyloxycarbonyl-L-cystine 
• 13961-96-1 (Z-Cys-NH₂)2 

Relevant articles and documents

Highly Selective Sub-Nanomolar Cathepsin S Inhibitors by Merging Fragment Binders with Nitrile Inhibitors

Pharmacological inhibition of cathepsin S (CatS) allows for a specific modulation of the adaptive immune system and many major diseases. Here, we used NMR fragment screening and crystal structure-aided merging to synthesize novel, highly selective CatS inhibitors with picomolar enzymatic Ki values and nanomolar functional activity in human Raji cells. Noncovalent fragment hits revealed binding hotspots, while the covalent inhibitor structure-activity relationship enabled efficient potency optimization.

Visible-Light-Mediated S?H Bond Insertion Reactions of Diazoalkanes with Cysteine Residues in Batch and Flow

We describe the application of S?H bond insertion reactions of aryl diazoacetates with cysteine residues that enabled metal-free, S?H functionalization under visible-light conditions. Moreover, this process could be intensified by a continuous-flow photomicroreactor on the acceleration of the reaction (6.5 min residence time). The batch and flow protocols described were applied to obtain a wide range of functionalized cysteine derivatives and cysteine-containing dipeptides, thus providing a straightforward and general platform for their functionalizations in mild conditions. (Figure presented.).

Application of a novel small scale UV LED photochemical batch reactor for the thiol-yne reaction

The application of a novel small scale UV LED photochemical batch reactor for the thiol-yne click reaction was investigated. Optimization of the reaction conditions yielded high conversions. Finally, the methodology could be successfully expanded to the one pot insertion of functionalized alkynes into the disulfide bond of a cysteine derivative.

Glycopolypeptides with a redox-triggered helix-to-coil transition

Conformation-switchable glycopolypeptides were prepared by the living polymerization of glycosylated l-cysteine-N-carboxyanhydride (glyco-C NCA) monomers. These new monomers were prepared in high yield by coupling of alkene-terminated C-linked glycosides of d-galactose or d-glucose to l-cysteine using thiol-ene "click" chemistry, followed by their conversion to the corresponding glyco-C NCAs. The resulting glycopolypeptides were found to be water-soluble and α-helical in solution. Aqueous oxidation of the side-chain thioether linkages in these polymers to sulfone groups resulted in disruption of the α-helical conformations without loss of water solubility. The ability to switch chain conformation and remain water-soluble is unprecedented in synthetic polymers, and allows new capabilities to control presentation of sugar functionality in subtly different contexts.

Acyl transfer from carboxylate, carbonate, and thiocarbonate esters to enzymatic and nonenzymatic thiolates

Transglutaminases (EC 2.3.2.13) (TGases) catalyze calcium-dependent acyl transfer reactions between peptide-bound glutamine residues as acyl donors and peptide-bound lysine residues as acyl acceptors, resulting in the formation of intermolecular ε-(γ-glutamyl)lysine crosslinks. The mechanistic details of its "ping-pong" transamidation reaction remain unknown. In particular, few studies have been published probing the nucleophilicity of TGase using acyl-donor substrates of varied electrophilicity. Herein we report the synthesis of activated esters of carbonates, carbamates, and thiocarbonates and their reactions with simple thiols, as a nonenzymatic point of reference, and with the catalytic cysteine residue of guinea pig liver TGase. Our kinetic results show that the simple substitution of a side chain methylene unit by oxygen or sulphur had a surprising effect on both substrate affinity and acylation reactivity. Furthermore, they provide unexpected insight into the importance of a side chain heteroatom for conferring affinity for tissue TGase as well as revealing an interesting class of irreversible inhibitors.

Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.

New 2-methylisothiazolones

New N,N′-bis(alkoxycarbonyl)-L-cystine bis(methylamides) 4a, 4b and N,N′-bis(benzyloxycarbonyl)-L-cystine bis(methylamide) 4c have been synthesized by mixed anhydride method from the essential amino acid L-cystine 1 in good yield. These cystine bis(methylamides) 4a,b,c have been cyclized with sulfuryl chloride. New 2-methyl-4-amino-3-isothiazolone and 5-chloro-2-methyl-4-amino-3-isothiazolone hydrobromide salts 7, 8 have been obtained by deacylation of 2-methyl-4-(benzyloxycarbonyl)amino-3-isothiazolone 5c and 5-chloro-2-methyl-4-(benzyloxycarbonyl)amino-3-isothiazolone 6c with hydrogen bromide in acetic acid. The microbicidal effect of the new 2-methyl-3-isothiazolones 5a,b,c; 6a,b,c; 7 and 8 compounds obtained by the above method has been investigated.

Protein folding: The synthesis and conformational studies on cystinyl- cystinyl-cystine [-CSSCCSSCCSSC-] a novel cross linking motif

The cysteine capped, ends protected cross linked motifs 6 and 7, arising from pairs of proximally placed cysteines wherein within a 22 atom framework are inscribed 3 disulphide bridges and 2 peptide linkage, have been prepared and their conformations derived by detailed 1H NMR studies and molecular modeling protocols, where excellent agreement was seen. Both compounds 6 and 7 possess a C2 symmetric hydrogen bonded pair involving the peptide NH and the CO of the proximate N-protecting group (Boc or Z). The nature of the latter profoundly influences the conformation. Thus, in 6 where the unit is Boc a bend conformation was promoted by hydrophobic interactions; alternatively in 7 with a Z-protecting group the conformation was linear. Compounds 6 and 7 have much promise in diverse aspects of protein design.

New diastereoselective synthesis of protected meso-lanthionine with discrimination of the chiral centers

A synthesis of meso-lanthionine with discrimination of the chiral centers is reported. Two cysteine residues of opposite configuration and with orthogonal protections are temporarily and reversibly linked in order to promote the formation of an intramolecular disulfide bridge thus avoiding symmetrization reactions during the sulfur extrusion step.