96289-13-3

Upstream product

• 6968-11-2 N,N'-bis(benzyloxycarbonyl)-L-cystine 
• 52-90-4 L-Cysteine 
• 57710-80-2 1-benzyloxycarbonyl-1Hbenzo[d][1.2.3]triazole 
• 2640-52-0 N-(Carbobenzoxy)-S-tert-butyl-L-cysteine 
• 501-53-1 benzyl chloroformate 
• 3422-03-5 benzyloxycarbonyl azide 
• 65798-29-0 Z-Cys(NPS) 

Downstream Products

• 6886-38-0 S-(2,2,2-Trifluor-1-benzamino-ethyl)-N-benzyloxycarbonyl-L-cystein 
• 57122-35-7 N-Benzyloxycarbonyl-S-cyanoformyl-L-cystein 
• 55281-66-8 (10aS)-3c-benzyloxycarbonylamino-10,10-dimethyl-4-oxo-3,4-dihydro-2H,10H-[1,3]thiazino[3,2-a]indole-10ar-carboxylic acid ethyl ester 
• 55281-66-8 (10aR)-3t-benzyloxycarbonylamino-10,10-dimethyl-4-oxo-3,4-dihydro-2H,10H-[1,3]thiazino[3,2-a]indole-10ar-carboxylic acid ethyl ester 
• 7697-01-0 Ethyl-N,N'-bis-carbobenzoxy-L-cystinyl-monoglycinat 
• 6776-25-6 S-(2,2,2-Trifluor-1-benzyloxycarbonyl-ethyl)-N-benzyloxycarbonyl-L-cystein 
• 6304-83-2 monobenzyloxycarbonyl-L-cystine 
• 6968-11-2 N,N'-bis(benzyloxycarbonyl)-L-cystine 
• 39994-69-9 S-Acetyl-N-[(Phenylmethoxy)carbonyl]-L-cysteine 
• 7697-00-9 1-Carboxy-5-methoxycarbonyl-1-benzyloxycarbonylamino-3,4-dithiopentan 
• 4526-91-4 N--glycin-ethylester 
• 127955-73-1 {(R)-2-{(R)-2-Benzyloxycarbonylamino-2-[N'-(2-chloro-ethyl)-N'-methyl-hydrazinocarbonyl]-ethyldisulfanyl}-1-[N'-(2-chloro-ethyl)-N'-methyl-hydrazinocarbonyl]-ethyl}-carbamic acid benzyl ester 
• 57213-09-9 N-α-Benzyloxycarbonyl-(L,D)-lanthionin 
• 110143-61-8 N-(benzyloxycarbonyl)-L-cysteine diphenylmethyl ester 

Relevant academic research and scientific papers

The Wittig bioconjugation of maleimide derived, water soluble phosphonium ylides to aldehyde-tagged proteins

Herein we disclose the transformation of maleimides into water-soluble tris(2-carboxyethyl)phosphonium ylides and their subsequent application in the bioconjugation of protein- and peptide-linked aldehydes. The new entry into Wittig bioconjugate chemistry proceeds under mild conditions and relies on highly water soluble reagents, which are likely already part of most biochemists' inventory. This journal is

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.).

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.

Cysteinoyl- and Cysteine-containing Dipeptidoylbenzotriazoles with Free Sulfhydryl Groups: Easy Access to N-terminal and Internal Cysteine Peptides

N-Protected cysteines 4a-c each with a free sulfhydryl group were prepared in 70-75% yields by treatment of l-cysteine with 1-(benzyloxycarbonyl) benzotriazole (Cbz-Bt) 1a, N-(tert-butyloxy-carbonyl)benzotriazole (Boc-Bt) 1b, and 1-(9-fluorenylmethoxy-carbonyl)benzotriazole (Fmoc-Bt) 1c, respectively. N-Protected, free sulfhydryl cysteines 4a-c were then converted into the corresponding N-protected, free sulfhydryl cysteinoylbenzotriazoles 7a-c (70-85%), which on treatment with diverse amino acids and dipeptides afforded the corresponding N-protected, free sulfhydryl N-terminal cysteine dipeptides 8a-e and tripeptides 8f-h in 73-80% yields. N-Protected, free sulfhydryl cysteine-containing dipeptides 9a,b were converted into the corresponding N-protected, free sulfhydryl dipeptidoylbenzotriazoles 10a,b (69-81%), which on treatment with amino acids, dipeptides, and a tripeptide afforded internal cysteine tripeptides 11a-c, tetrapeptides 11d,e and pentapeptide 11f, each containing a N-protected, free sulfhydryl groups in 70-90% yields under mild conditions. Treatment of N-protected, free sulfhydryl cysteinoylbenzotriazole 7a with diamines 12a,b afforded directly the cysteine-containing disulfide-bridged cyclic peptides 14a,b in 50% yields. Novel and stable N-protected, free sulfhydryl, cysteine-containing dipeptidoylbenzotriazoles formed internal cysteine containing N-protected free sulfhydryl tripeptides, tetrapeptides, and pentapeptide under mild reaction conditions in good yields that can be useful in the syntheses of other naturally occurring or biologically active cysteine-containing peptides.

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.

COMPOUNDS CONTAINING A FUSED BICYCLE RING AND PROCESSES THEREFOR

Compounds of the formula STR1 wherein X is O or S--(O) t ; n is one or two; m is zero or one; Y is CH 2, O, or S--(O) t provided that Y is O or S--(O) t only when m is one; and A is STR2 are dual inhibitors of NEP and ACE. Compounds wherein A is STR3 are selective ACE inhibitors. Also disclosed are methods of preparation and intermediates.

Angiotensin-Converting Enzyme Inhibitors: Perhydro-1,4-thiazepin-5-one Derivatives

α-amino>-5-oxoperhydro-1,4-thiazepin-4-yl>acetic acids (monoester monoacids) and their dicarboxylic acids having the hydrophobic substituents at the 2- or 3-position of the thiazepinone ring were prepared and assayed for angiotensin-converting enzyme (ACE) inhibitory activity.The dicarboxylic acids having the pseudoequatorial amino groups at the 6-position and the pseudoequatorial hydrophobic substituents at the 2- or 3-position of the chair conformation of the thiazepinone ring had potent in vitro inhibitory activity.The monoester monoacids having the hydrophobic substituents at the 2-position suppressed pressor response to angiotensin I for a longer duration than those having the substituents at the 3-position when administered orally.The structure-activity relationship was studied by conformational energy calculations of the thiazepinone ring.