86961-90-2

Basic information

• Product Name: S-benzyl-N-benzyloxycarbonyl-cysteinyl=>tyrosyl=>isoleucine methyl ester
• CAS NO: 86961-90-2
• Molecular Weight: 635.781
• Mol File: 86961-90-2.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: S-benzyl-N-benzyloxycarbonyl-cysteinyl=>tyrosyl=>isoleucine methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: S-benzyl-N-benzyloxycarbonyl-cysteinyl=>tyrosyl=>isoleucine methyl ester(86961-90-2)
• EPA Substance Registry System: S-benzyl-N-benzyloxycarbonyl-cysteinyl=>tyrosyl=>isoleucine methyl ester(86961-90-2)

Safety Data

• Hazardous Substances Data: 86961-90-2(Hazardous Substances Data)

Upstream product

• 2577-46-0 L-isoleucine methyl ester 
• 39621-64-2 S-benzyl-N-[(benzyloxy)carbonyl]cysteinyltyrosine 
• 16152-80-0 benzyloxycarbonyl-S-benzylcysteinyl-tyrosine ethyl ester 
• 18598-74-8 methyl L-isoleucinate hydrochloride 
• 60-18-4 L-tyrosine 
• 19519-00-7 N-(S-benzyl-N-benzyloxycarbonyl-L-cysteinyl)-L-tyrosine methyl ester 
• 73-32-5 L-isoleucine 
• 3257-18-9 benzyloxycarbonyl-S-benzylcysteine 
• 1080-06-4 L-Tyr-OMe 

Relevant articles and documents

FREE CHYMOTRYPSIN-CATALYZED SYNTHESIS OF PEPTIDE BOND AN ALIPHATIC ALCOHOLS WITH LOW WATER CONTENT

The effect of water content on free chymotrypsin-catalyzed reaction of Ac-Tyr-OEt with HBr*Gly-NH2 in triethylamine-containing 2-propanol was studied.Maximum yield of dipeptide Ac-Tyr-Gly-NH2 was obtained in 2-propanol with 2percent of water.Lower water content retards the reaction.Although higher water content accelerates the process, the yield of the dipeptide is reduced by enzymatically catalyzed hydrolysis of Ac-Tyr-OEt.The studied reaction proceeds analogously also in other aliphatic alcohols with low content of water except in methanol; it does not take place in dimethylformamide or dimethyl sulfoxide containing 2percent or 20percent of water.In 2-propanol with 2percent or 5percent of water, syntheses of the protected amino-terminal oxytocine and vasopressin tripeptide as well as other model peptides, were studied.In all the described experimetns, α-chymotrypsin without any stabilization or immobilization was employed.