80645-37-0

Upstream product

• 16677-09-1 Z-L-Tyr-Gly-OMe 
• 15373-56-5 glycyl-L-phenylalanyl-L-leucine 
• 3303-55-7 L-Phe-Leu 
• 34695-67-5 Z-Tyr-Gly-Gly-OEt 
• 16679-94-0 N-[(phenylmethoxy)carbonyl]-L-tyrosine 
• 13512-31-7 N-(benzyloxycarbonyl)-L-tyrosine methyl ester 
• 74072-21-2 N-[N-(N-benzyloxycarbonyl-L-tyrosyl)-glycyl]-glycine 
• 215095-19-5 [(S)-2-(4-Hydroxy-phenyl)-1-({[({(S)-1-[(S)-3-methyl-1-(N'-phenyl-hydrazinocarbonyl)-butylcarbamoyl]-2-phenyl-ethylcarbamoyl}-methyl)-carbamoyl]-methyl}-carbamoyl)-ethyl]-carbamic acid benzyl ester 

Downstream Products

• 125816-06-0 (S)-2-[(S)-2-(2-{2-[(S)-2-Benzyloxycarbonylamino-3-(4-hydroxy-phenyl)-propionylamino]-acetylamino}-acetylamino)-3-phenyl-propionylamino]-4-methyl-pentanoic acid 2-cyano-ethyl ester 

Relevant academic research and scientific papers

Enzymatic syntheses of N-protected Leu-enkephalin and some oligopeptides in organic solvents

Enzymatic syntheses of bioacitive pentapeptide, N-protected Leu- enkephalin and some other oligopeptides in organic solvents were studied. The stereoselectivity of the enzymatic reaction was examined by using racemic substrates. Different enzymes, solvent systems and protecting groups were compared. The importance of the essential water was addressed. The side chain of tyrosine was not protected during all the enzymatic reactions, P-DL-AlaOY (P=Z or Boc, Y=H or Me) and P-DL-TyrOEt were coupled with GlyNHNHPh by papain and α-chymotrypsin in mixed solvent or organic solvent to obtain the expected optically pure products P-L-AlaGlyNHNHPh and P-L-TyrGlyNHNHPh respectively in good yield. Two sweetener precursors, ZAspXaaOR (XaaOR=PheOMe or AlaOcHex) were synthesized by thermolysin in tert-amyl alcohol and some reaction conditions were optimized to get the best yield. Full enzymatic synthesis of N-protected Leu-enkephalin ZTyrGlyGlyPheLeuOH was investigated using α-chymotrypsin and thermolysin as catalysts in dichloromethane and tert-amyl alcohol.

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.