65118-56-1

Upstream product

• 3235-14-1 (S)-2-((S)-2-Benzyloxycarbonylamino-propionylamino)-3-phenyl-propionic acid methyl ester 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 2768-53-8 N-benzyloxycarbonyl-L-alanyl-L-phenylalanine 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 1142-20-7 N-Cbz-Ala 
• 687-51-4 H-L-Leu-NH₂ 
• 92278-79-0 Z-Ala-Phe-OBzl-SO₃Na 

Relevant academic research and scientific papers

Peptide Synthesis Mediated by Immobilized and Viable Baker's Yeast in Reverse Micelles: Synthesis of Leucine Enkephalin Analogues

Cells of baker's yeast (Saccharomyces cerevisiae NCIM 3305) immobilized in calcium alginate beads are found to be viable in reverse micelles of bis(2-ethylhexyl)sulphosuccinate sodium salt 1 in iso-octane for days and were used for the first time for pept

Chymotrypsin suspended in organic solvents with salt hydrates is a good catalyst for peptide synthesis from mainly undissolved reactants

Chymotrypsin powder suspended in organic solvents in the presence of Na2CO3.10H2O catalyses peptide synthesis from X-Ala-Phe-OMe and Leu-NH2 (X = Boc or Z). The reaction proceeds best in the most non-polar solve

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.

Facile amide bond formation from esters of amino acids and peptides catalyzed by alkaline protease in anhydrous tert-butyl alcohol using ammonium chloride/triethylamine as a source of nucleophilic ammonia

An industrial alkaline protease 'Alcalase', stable and active in tert-butyl alcohol, was used to catalyze the synthesis of N-protected amino acids or peptide amides in anhydrous tert-butyl alcohol using ammonium chloride/triethylamine as source of nucleophilic ammonia

The 2-Thiosulfatoethyl Group as Solubilizing Protective Group in Enzymatic Peptide Synthesis

Amino acid (2-thiosulfatoethyl esters) 4 can be prepared from amino acid (2-chloroethyl esters) by nucleophilic exchange of halogen for thiosulfate.Coupling of the esters 4 with Z-protected amino acids gives the water-soluble Z-dipeptide esters 5 which re

Model Studies on Carboxypeptidase Y Catalyzed Peptide Synthesis in an Aqueous-Organic Two-Phase System

Carboxypeptidase Y catalyzes in a biphasic system containing carbon tetrachloride and carbonate buffer the reaction of Z-Phe-OMe and various Z- and Boc-protected dipeptide methyl esters with Val-NH2 and Leu-NH2 respectively.This method has been applied to

Peptide Synthesis by Means of Immobilized Enzymes II. Immobilized Trypsin, Thermolysin and Papain

Model studies were performed on the utility of covalently immobilized trypsin, thermolysin and papain for peptide bond formation.Trypsin and thermolysin catalyzed the formation of peptide bonds with nearly the same efficiency as the soluble proteases and they could be re-used successfully for further coupling experiments.The possibility of using immobilized trypsin and papain for kinetically controlled peptide bond formation was investigated.With the serine type enzyme trypsin excellent product yields were obtained starting with ester carboxyl components and an economical ratio of substrates.Experiments with the thiol protease papain were unsatisfactory because the once formed product is hydrolyzed as fact as the starting ester substrate used. - Keywords: Immobilized enzymes; Papain; Peptide synthesis; Thermolysin; Trypsin

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