96289-13-3

Basic information

• Product Name: Cysteine, N-[(phenylmethoxy)carbonyl]-
• CAS NO: 96289-13-3
• Molecular Formula: C11H13NO4S
• Molecular Weight: 255.295
• Mol File: 96289-13-3.mol
• Article Data: 7

Chemical Properties

• CAS DataBase Reference: Cysteine, N-[(phenylmethoxy)carbonyl]-(CAS DataBase Reference)
• NIST Chemistry Reference: Cysteine, N-[(phenylmethoxy)carbonyl]-(96289-13-3)
• EPA Substance Registry System: Cysteine, N-[(phenylmethoxy)carbonyl]-(96289-13-3)

Safety Data

• Hazardous Substances Data: 96289-13-3(Hazardous Substances Data)

Upstream product

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

Downstream Products

• 6886-38-0 S-(2,2,2-Trifluor-1-benzamino-ethyl)-N-benzyloxycarbonyl-L-cystein 
• 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 
• 298712-65-9 N,N'-bis(benzyloxycarbonyl)-L-cystine bis(tetradecylamide) 
• 1363385-99-2 C₂₈H₃₇NO₁₅S 
• 1363386-00-8 C₂₈H₃₇NO₁₅S 
• 1363385-97-0 C₂₈H₃₇NO₁₃S 
• 1363385-96-9 C₂₈H₃₇NO₁₃S 
• 1385775-64-3 N-Cbz-L-Cys-L-Ser-OH 
• 1385775-66-5 N-Cbz-L-Cys-Gly-Gly-OH 
• 1385775-67-6 N-Cbz-L-Cys-L-Leu-Gly-OH 
• 1385775-68-7 N-Cbz-L-Cys-Gly-L-Ala-OH 

Relevant articles and documents

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

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.