4526-84-5

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 2087-41-4 glycyl glycine ethyl ester hydrochloride 
• 2440-94-0 quinolin-8-yl ester of N-benzyloxycarbonyl-L-phenylalanine 
• 627-74-7 glycylglycine ethyl ester 
• 126028-14-6 2,2,2-trifluoroethyl ((benzyloxy)carbonyl)-L-phenylalaninate 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 

Downstream Products

• 64967-39-1 N?[3?(2?furyl)acryloyl]-L-phenylalanylglycylglycine 

Relevant academic research and scientific papers

Synthesis of a precursor of bioactive pentapeptide OGP-(10-14) and the fragment of enkephalin catalyzed by MCM-22 immobilized or free proteases in organic solvents

Full enzymatic synthesis of a precursor of osteogenic growth peptide fragment (10-14), Z-Tyr-Gly-Phe-Gly-Gly-OEt, was accomplished using immobilized proteases on molecular sieve MCM-22 by adsorption as catalyst via 3+2 synthetic route for the first rime. The reuse time of immobilized enzyme was dependent on concrete reaction system. Compared with free enzyme, the reaction rate catalyzed by immobilized enzyme was remarkably enhanced and its synthetic yield was also increased in most cases. The effects of water content and the added amount of Et3N on synthesis of fragments of bioactive peptides including OGP-(10-14) and enkephalin by immobilized enzymes were different from free enzyme.

Full enzymatic synthesis of a precursor of bioactive pentapeptide OGP(10-14) in organic solvents

Full enzymatic synthesis of a fragment of osteogenic growth peptide (OGP), a precursor of bioactive pentapeptide OGP(10-14) (Z-TyrGlyPheGlyGlyOEt), was accomplished by papain, α-chymotrypsin, and thermolysin via 2+3 or 3+2 synthetic routes in organic solvents for the first time. The factors influencing the enzymatic synthesis of fragments of OGP(10-14) were systematically studied.

Carbohydrate Protease Conjugates: Stabilized Proteases for Peptide Synthesis

The synthesis of oligopeptides using stable carbohydrate protease conjugates (CPCs) was examined in acetonitrile solvent systems.CPC was used for the preparation of peptides containing histidine, phenylalanine, tyrosine, and tryptophan in the P1 position in 60-93percent yield.The CPC was used to synthesize peptides containing both hydrophilic and hydrophobic amino acids.The P2 specificity of papain for aromatic residues was utilized for the 2 + 3 coupling of Z-Tyr-Gly-OMe to H2N-Gly-Phe-Leu-OH to generate the leucine enkephalin derivative in 79percent yield.Although papain is nonspecific for the hydrolysis of N-benzyloxycarbonyl amino acid methyl esters in aqueous solution, the rates of synthesis for these derivatives with nucleophile leucine tert-butyl ester differed by nearly 2 orders of magnitude.CPC was used to prepare the aspartame precursor Z-Asp-Phe-OMe in 90percent yield.The increased stability of CPCs prepared from periodate-modified poly(2-methacrylamido-2-deoxy-D-glucose), poly(2-methacrylamido-2-deoxy-D-galactose), and poly(5-methacrylamido-5-deoxy-D-ribose), carbohydrate materials designed to increase the aldehyde concentration in aqueous solution, suggests that the stability of CPCs is directly related to the aldehyde concentration of the carbohydrate material.Periodate oxidation of poly(2-methacrylamido-2-deoxy-D-glucose) followed by covalent attachment to α-chymotrypsin gave a CPC with catalytic activity in potassium phosphate buffer at 90 deg C for 2 h.