79113-78-3

Upstream product

• 3235-14-1 (S)-2-((S)-2-Benzyloxycarbonylamino-propionylamino)-3-phenyl-propionic acid methyl ester 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 1142-20-7 N-Cbz-Ala 
• 28819-05-8 (S)-2-benzyloxycarbonylamino-propionic acid methyl ester 
• 3303-55-7 L-Phe-Leu 
• 61-90-5 L-leucine 

Downstream Products

• 1639120-79-8 Cbz-Ala-Phe-Leu-Leu-OMe 

Relevant academic research and scientific papers

A one-pot saponification-coupling sequence suitable for C-terminus peptide elongation using lithium carboxylates

An efficient procedure has been developed for the saponification of common peptide esters, followed by straightforward coupling of the lithium carboxylate. Adding some water to the reaction medium gave faster saponification and did not interfere with the coupling reagent. As peptide chemistry constitutes a major application of the amidation reaction, amino acid substrates were chosen for this study, monitoring both yields and epimerization of the peptides obtained. Georg Thieme Verlag Stuttgart New York.

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.

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

ENZYME-CATALYZED PEPTIDE SYNTHESIS IN BIPHASIC AQUEOUS-ORGANIC SYSTEMS

A preparative protease-catalysed peptide synthesis in biphasic aqueous-organic systems is described.This approach using both free as well as immobilized proteases as catalysts provides high yields and includes the possibility to re-utilize the enzymes.