99998-12-6

Upstream product

• 57710-80-2 1-benzyloxycarbonyl-1Hbenzo[d][1.2.3]triazole 
• 850232-61-0 benzyl N-[(1R)-2-(1H-1,2,3-benzotriazol-1-yl)-2-oxo-1-(sulfanylmethyl)ethyl]carbamate 
• 63-91-2 L-phenylalanine 
• 3693-93-4 (Z-L-Cys-L-PheOMe)2 
• 501-53-1 benzyl chloroformate 
• 6968-11-2 N,N'-bis(benzyloxycarbonyl)-L-cystine 
• 339175-29-0 (Z-L-Cys-L-PheOH)2 

Relevant academic research and scientific papers

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.