102988-95-4

Upstream product

• 1164-16-5 Z-L-Tyr-OH 
• 543-27-1 isobutyl chloroformate 
• 501-53-1 benzyl chloroformate 
• 13512-31-7 N-(benzyloxycarbonyl)-L-tyrosine methyl ester 

Downstream Products

• 150650-87-6 1-(N-benzyloxycarbonyl-L-tyrosyl)-2-methyl-2-tert-butoxycarbonyl hydrazine 
• 102683-29-4 N-(benzyloxycarbonyl)-L-tyrosyl-L-arginine methyl ester 
• 188196-22-7 L-tyrosyl-D-alanyl-p-fluoro-L-phenylalanyl-L-phenylalaninamide 
• 102683-28-3 N-(benzyloxycarbonyl)-L-tyrosyl-D-arginine methyl ester 

Relevant academic research and scientific papers

Direct N-glycan profiling in the presence of tryptic peptides on MALDI-TOF by controlled ion enhancement and suppression upon glycan-selective derivatization

Even though the formidably laborious and time-consuming nature of oligosaccharide analysis limits certain attempts to analyze the glycosylation profile, the significant elucidation of carbohydrate modifications is largely dependent on it. Aiming to substa

Frakefamide, an analgesic tetrapeptide: Development of a pilot-plant-scale process

A pilot-plant-process is described where frakefamide × HCl (L-tyrosyl-D-alanyl-p-fluoro-L-phenylalanyl-L-phenylalanin-amide hydrochloride) was synthesised from its amino acid monomers in seven steps. The synthesis was performed in 70-L equipment, and the

New amino acid porphyrin derivatives. Part I: Synthesis

In order to obtain molecules that can bind to specific DNA-sequences, several new tri-(N-methyl-4-pyridiniumyl)porphyrins bearing an amino acid or peptide side-chain on the fourth meso aromatic substituent have been synthesized by efficient coupling of a

Peptidyl and azapeptidyl methylketones as substrate analog inhibitors of papin and cathepsin B

Peptidyl methylketones containing Phe, Tyr, Tyr(I), Tyr(I2), Leu and Ile in P2 were synthesized and tested as substrate analog revesible of papain and bovine spleen cathepsin B.The most effective cathepsin B inhibitor contained Tyr(I2) and displayed an inhibition constant of 4.7 μM at pH 6.8 and 25 deg C, while Leu or Ile gave practically inert analogs.Replacement of the amino acids in P2 with the analogues α-azaamino acids, as well as the glycine in P1 with α-azaglycine, led to complete loss of inhibiting activity.Introducing alkoxy substituents at themethyl adjacent to the ketone group generally resulted in more effective inhibitors, with inhibition constants in the micromolar range for both papin and cathepsin B. - Keywords: enzyme inhibiting activity; cysteine proptease; slow binding; peptidyl methylketone; azapeptidyl methylketone; papain; cathepsin B

Synthesis and inhibiting activities of 1-peptidyl-2-haloacetyl hydrazines toward cathepsin B and calpains

Twenty-four 1-peptidyl-2-haloacetyl hydrazines which can be considered azapeptide halomethanes were synthesized and tested as models of cathepsin B, calpain I and calpain II inhibitors.Reagents designed for cathepsin B inactivation include Z-Tyr, Z-Tyr(I)

Iodo and diiodotyrosine epoxysuccinyl derivatives as selective inhibitors of cathepsin B

Eight new analogs of L-trans-epoxysuccinyl-L-leucylamido(3-methyl)butane (E-64-c) containing Phe, Tyr, Tyr(I) or Tyr(I2) in place of Leu, were synthesized and tested as inhibitors of papain, bovine spleen cathepsin B, calpain I and II from porc

Enzyme-Catalyzed Irreversible Formation of Peptides Containing D-Amino Acids

Procedures have been developed for the preparation of dipeptides Z-L-Tyr-D-X and Z-L-Phe-D-X using Z-L-Tyr-OMe (or Z-L-Phe-OMe) and D-amino acid esters or amides (D-X) as substrates and soluble or immobilized α-chymotrypsin as a catalyst.The formation of each of these peptides in miscible or immiscible organic solvent-water systems in a kinetically controlled approach is virtually irreversible with no side reactions or racemization.Kinetic studies indicate that D-amino acid esters are about 100 times that of water and 10percent that of L-amino acid esters as a nucleophile in deacylation reactions.The effects of pH, organic solvents, temperature, and substrate and enzyme concentrations on the yield and the stability of the enzyme in syntheses have been studied and the results compared with those in the enzyme-catalyzed formation of L-L-dipeptides.