17187-05-2

Upstream product

• 52641-32-4 N-benzyloxycarbonyl-L-phenylalanyl chloride 
• 598-41-4 H-Gly-NH₂ 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 3272-95-5 Z-L-Phe p-chlorophenyl ester 
• 1668-10-6 glycinamide hydrochloride 
• 126028-14-6 2,2,2-trifluoroethyl ((benzyloxy)carbonyl)-L-phenylalaninate 
• 60379-01-3 N-(benzyloxycarbonyl)-L-phenylalanine benzyl ester 
• 4816-89-1 Cbz-Phe-OCH₂CONH₂ 
• 1161-13-3 N-Cbz-L-Phe 

Downstream Products

• 5184-17-8 N-benzyloxycarbonyl-L-phenylalanylglycine methyl ester 
• 38678-61-4 H-L-Phe-Gly-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.

Chemically modified "polar patch" mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: Designing combinatorial biocatalysts

A significant enhancement of the applicability of the serine protease subtilisin Bacillus lentus (SBL) in peptide synthesis was achieved by using the strategy of combined site-directed mutagenesis and chemical modification to create chemically modified mu

Synthesis and biological evaluation of analogues of the antibiotic pantocin B

Strains of the bacteria Erwinia herbicola produce antibiotics that effectively control E. amylovora, the bacterial pathogen responsible for the plant disease fire blight. Pantocin B was the first of these antibiotics to be characterized, and a flexible sy

Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis

Site-selective glycosylation at position 166 at the base of the primary specificity S1 pocket in the serine protease subtilisin Bacillus lentus (SBL) created glycoproteins that are capable of catalyzing the coupling reactions of not only L- ami

Expanded structural and stereospecificity in peptide synthesis with chemically modified mutants of subtilisin

Employing the strategy of combined site directed mutagenesis and chemical modification, we previously generated chemically modified mutant enzymes (CMMs) of subtilisin Bacillus lentus (SBL). We now report the use of these SBL-CMMs for peptide coupling rea

Pronase catalysed peptide syntheses

A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.

Immobilized Aspergillus Oryzae Protease Catalyzed Formation of Peptide Bonds in Organic Solvent

Immobilized Aspergillus oryzae protease (AOP) catalyzed the formation of peptide bonds between N-protected amino acids and amino acid esters or amides in ethyl acetate. The influences of pH and reaction time on the coupling of Boc-L-Tyr and Gly-NH2/

Exploitation of subtilisin BPN' as catalyst for the synthesis of peptides containing noncoded amino acids, peptide mimetics and peptide conjugates

The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts nume

α-Chymotrypsin-catalysed peptide synthesis using activated esters as acyl donors

The coupling efficiency in α-chymotrypsin-catalysed peptide synthesis is greatly improved by the use of activated esters such as the 2,2,2-trifluoroethyl ester as acyl donor instead of the conventional methyl ester; this approach is useful for the incorporation of non-protein amino acids into peptides.