119874-29-2

Basic information

• Product Name: {(R)-2-Benzylsulfanyl-1-[(S)-1-((S)-1-carbamoyl-2-phenyl-ethylcarbamoyl)-2-(4-hydroxy-phenyl)-ethylcarbamoyl]-ethyl}-carbamic acid benzyl ester
• CAS NO: 119874-29-2
• Molecular Weight: 654.787
• Mol File: 119874-29-2.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: {(R)-2-Benzylsulfanyl-1-[(S)-1-((S)-1-carbamoyl-2-phenyl-ethylcarbamoyl)-2-(4-hydroxy-phenyl)-ethylcarbamoyl]-ethyl}-carbamic acid benzyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: {(R)-2-Benzylsulfanyl-1-[(S)-1-((S)-1-carbamoyl-2-phenyl-ethylcarbamoyl)-2-(4-hydroxy-phenyl)-ethylcarbamoyl]-ethyl}-carbamic acid benzyl ester(119874-29-2)
• EPA Substance Registry System: {(R)-2-Benzylsulfanyl-1-[(S)-1-((S)-1-carbamoyl-2-phenyl-ethylcarbamoyl)-2-(4-hydroxy-phenyl)-ethylcarbamoyl]-ethyl}-carbamic acid benzyl ester(119874-29-2)

Safety Data

• Hazardous Substances Data: 119874-29-2(Hazardous Substances Data)

Upstream product

• 16152-80-0 benzyloxycarbonyl-S-benzylcysteinyl-tyrosine ethyl ester 
• 65864-22-4 (S)-2-amino-3-phenylpropionamide hydrochloride 
• 3257-18-9 benzyloxycarbonyl-S-benzylcysteine 

Downstream Products

• 117509-66-7 H-Cys(Et)-Tyr-Phe-NH₂ 

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.