4816-89-1

Upstream product

• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 79-07-2 Chloroacetamide 
• 1161-13-3 N-Cbz-L-Phe 

Downstream Products

• 1161-13-3 N-Cbz-L-Phe 
• 29842-94-2 (S)-tert-butyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-4-methylpentanoate 
• 28944-94-7 (S)-methyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)propanoate 
• 106556-07-4 Z-Phe-Leu-Ala-NH₂ 
• 17430-32-9 N--(S)-α-methylbenzylamine 
• 17430-33-0 N--(R)-α-methylbenzylamine 
• 141056-54-4 N-benzyloxycarbonyl-L-phenylalanyl-L-phenylalaninamide 
• 143087-83-6 Z-L-Phe-L-Ala-L-Leu-NH₂ 
• 106556-09-6 Z-Phe-Phe-Ala-OCAM 
• 71450-10-7 benzyl N-((1S)-2-[(1S)-1-(aminocarbonyl)-3-(methylsulfanyl)propyl]amino-1-benzyl-2-oxoethyl)carbamate 
• 76264-55-6 Z-L-Phe-L-Ser-NH₂ 
• 69193-11-9 Z-L-Phe-L-Val-NH₂ 
• 17187-05-2 Z-L-phenylalanylglycinamide 
• 69193-13-1 Cbz-L-Phe-L-Leu-NH₂ 

Relevant academic research and scientific papers

Kinetically controlled peptide synthesis mediated by papain using the carbamoylmethyl ester as an acyl donor

A series of dipeptides were synthesized generally in good yields with carbamoylmethyl (Cam) esters as acyl donors in the presence of a cysteine protease, papain, immobilized on Celite. Several segment condensations were also achieved generally in high yields without danger of racemization and formation of the secondary-hydrolysis product. Moreover, partial sequences of some bioactive peptides were prepared through segment condensations, and aimed-at peptides were obtained generally in high yields without the racemization of C-terminal residues of the carboxyl components. Thus, the superiority of the Cam ester in the kinetically controlled peptide synthesis was once again ascertained in couplings mediated by the cysteine protease as in those catalyzed by the serine proteases reported earlier.

Superiority of the carbamoylmethyl ester as an acyl donor for the kinetically controlled amide-bond formation mediated by α-chymotrypsin

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed kinetically controlled peptide-bond formation is demonstrated in the couplings of an inherently poor amino acid substrate, Ala, with various amino acid residues as amino components and in the couplings of non-protein amino acids such as halogenophenylalanines as carboxylic components. Furthermore, this approach is applied to the amide-bond formation between an amino acid residue and a chiral amine, which is highly diastereoselective.

On the Use of Carboxamidomethyl Esters in the Protease-Catalyzed Peptide Synthesis

Carboxyamidomethyl esters (CAM esters) of Z-and Boc-protected alanine and phenylalanine were prepared in order to investigate their usefulness as substrates for α-chymotrypsin- and papain-catalyzed hydrolysis and peptide synthesis reactions.The easy removal of the CAM-C-protecting group under mild conditions and dependent on the enzyme specificity was demonstrated.Examples are given for the protease-catalyzed synthesis of various peptide derivatives using CAM esters as C- and N-components in aqueous-organic media.Comparatively short reaction times were observed. - Key words: Carboxyamidomethyl ester as C-protecting group; Enzymatic deprotection; Peptide synthesis; α-Chymotrypsin- and Papain-catalyzed peptide bond formation

CARBOXAMIDOMETHYL ESTERS (CAM ESTERS) AS CARBOXYL PROTECTING GROUPS

The carboxamidomethyl esters (CAM esters) are proposed for carboxyl protection in peptide synthesis.Amino acid CAM ester derivatives were easily prepared and showed good stability in the deblocking conditions of other common protecting groups used in pept