69193-15-3

Upstream product

• 687-51-4 H-L-Leu-NH₂ 
• 6206-42-4 N-benzyloxycarbonylglycyl-L-phenylalanine methyl ester 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 1145-81-9 ethyl 2-(benzyloxycarbonylamino)ethanoate 
• 38678-59-0 L-Phe-L-Leu-NH₂ 
• 169676-29-3 Z-Gly-L-Phe-O-CH₂CF₃ 
• 114006-17-6 Z-Gly-L-Phe-O-carbamoylmethyl 
• 1138-80-3 N-(Benzyloxycarbonyl)glycine 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 69193-13-1 Cbz-L-Phe-L-Leu-NH₂ 
• 1170-76-9 Z-Gly-(L)-Phe 

Downstream Products

• 84969-56-2 Z-Gly-Gly-L-Phe-L-Leu-NH₂ 
• 82948-92-3 [des-tyr¹]-leucine enkephalinamide 
• 71591-21-4 Z-Tyr-Gly-Gly-Phe-Leu-NH₂ 
• 71591-20-3 H-Gly-Phe-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.

α-chymotrypsin-catalysed segment condensations via the kinetically controlled approach using carbamoylmethyl esters as acyl donors in organic media

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed segment condensations via the kinetically controlled approach is demonstrated in several model systems carried out in organic media with low water content. Furthermore, this approach is successfully applied to the construction of the Leu-enkephalin sequence via a 4 + 1 segment coupling.

Superiority of the carbamoylmethyl ester as an acyl donor for the protease-catalyzed kinetically controlled peptide synthesis in organic media: Application to segment condensations

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalyzed kinetically controlled peptide synthesis was demonstrated in several segment condensations carried out in organic media with low water content. Then this approach was successfully applied to the construction of the Leuenkephalin sequence via the 4 + 1 segment condensation.

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.

Continuous synthesis of a tripeptide by successive condensation and transesterification catalyzed by two immobilized proteinases in organic solvent.

The tripeptide Z-GlyPheLeuNH2 was continuously synthesized in a high yield from three amino acid derivatives, Z-Gly, PheOMe, and LeuNH2, by immobilized thermolysin (IMT) and immobilized alpha-chymotrypsin (IMC) in an organic solvent, ethyl acetate. The op

Papain Catalysed Peptide Synthesis: Control of Amidase Activity and the Introduction of Unusual Amino Acids

Procedures for the papain catalysed synthesis of peptides containing D-amino acids and derivatives with control of the enzyme's amidase activity have been developed.

Peptide Synthesis by Means of Immobilized Enzymes. I. Immobilized α-Chimotripsin

α-Chymotrypsin covalently bound to silica, enzacryl AA, and enzacryl AH catalyzes peptide bond formation between N-protected dipeptide methyl esters and H-Leu-NH2 with results similar to those with the free enzyme.The influence of water-miscible and water

Attempts for the Application of Thermitase as a Catalyst for Peptide Bond Formation

The utility of thermitase, a thermophilic proteolytic enzyme from Thermoactinomyces vulgaris, as a catalyst for peptide synthesis has been studied using several Nα-benzyloxycarbonyl dipeptide esters as carboxyl components and Leu-NH2 as nucleophile.Couplings were most successfull with substrates containing Met, Leu, Ala, Phe, Tyr in P1-position, and Val, Ala, Pro in P2, whereas the substrates with Val, Ile, Pro in P1 failed to couple. - Keywords: Enzymatic peptide synthesis; Thermitase

α-Chymotrypsin-catalyzed Synthesis of Tripeptide Amides in an Aqueous-Organic Two-phase System

α-Chymotrypsin catalyzes in a biphasic system containing an organic solvent and hydrogencarbonate buffer the reaction of Boc-Leu-Phe-OMe with X-NH2 (X=Leu, Met, Val) forming Boc-tripeptide amides.In the case of X=Leu the addition of ammoniumsulfate is advantageous and allows the use of carboxyl and amino component in equivalent amounts.By the same method Z-protected tripeptide amides can be prepared from Z-X-Phe-OMe (X=Ala, Leu, Val) and Leu-NH2 in good yields.In some case α-chymotrypsin-catalyzed peptide coupling is also possible, if the buffer solution is substituted for crystal water containing sodium carbonate.