62074-75-3

Basic information

• Product Name: L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-leucyl-
• CAS NO: 62074-75-3
• Molecular Formula: C17H25N3O4
• Molecular Weight: 335.403
• Mol File: 62074-75-3.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-leucyl-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-leucyl-(62074-75-3)
• EPA Substance Registry System: L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-leucyl-(62074-75-3)

Safety Data

• Hazardous Substances Data: 62074-75-3(Hazardous Substances Data)

Upstream product

• 7324-05-2 L-alanine amide 
• 124980-31-0 benzyloxycarbonyl-L-leucine benzyl ester 
• 33208-99-0 (S)-alaninamide hydrochloride 
• 126401-00-1 Cbz-D,L-Leu-OBzl 
• 51021-87-5 N-benzyloxycarbonyl-L-leucine methyl ester 

Relevant articles and documents

α-Chymotrypsin-catalyzed peptide synthesis in frozen aqueous solution using N-protected amino acid carbamoylmethyl esters as acyl donors

A kinetically controlled peptide synthesis catalyzed by α-chymotrypsin was performed in frozen aqueous solution (ice, -24 °C). The yield of the peptide was significantly improved by the use of the carbamoylmethyl (Cam) ester as the acyl donor instead of the conventional ethyl ester. The peptide yield increased up to ca. 90% when N-benzyloxycarbonyl (CBZ)-Phe-OCam and H-Phe-NH2 were used as the acyl donor and nucleophile, respectively. Such an improvement of the peptide yield in ice was also observed in the coupling of other CBZ-amino acid Cam esters as acyl donors. Furthermore, this approach was applied to the synthesis of peptides containing d-amino acids. The peptides such as CBZ-d-Phe-Phe-NH2, CBZ-Phe-d-Phe-NH2 and CBZ-d-Phe-d-Phe-NH2 were also obtained in excellent to moderate yields in ice. A high diastereoselectivity towards the l-l peptide was observed when the racemic amino acid Cam ester was used as the acyl donor in ice.

Kinetically Controlled Peptide Bond Formation in Anhydrous Alcohol Catalyzed by the Industrial Protease Alcalase

The industrial alkaline protease alcalase has been found to be very stable (half life > 5 days in ethanol or 2-methyl-2-propanol) and active in alcoholic solvents (except methanol).Procedures have been developed for alcalase-catalyzed, kinetically controlled peptide bond formation in anhydrous alcohol (ethanol, 2-methyl-2-propanol).Studies of the selectivity of an alcalase-catalyzed reaction show that only L-amino acid acyl donors are substrates at the p-1 subsite of alcalase; at the p-1' subsite both D- and L-amino acid nucleophiles are substrates.Other amino compounds such as benzylamine and phenylhydrazine are good nucleophiles.Studies of the effect of the water content of the reaction solution on the yield in the synthesis of Moz-Phe-Leu-NH2 showed that the 95percent yield obtained in anhydrous 2-methyl-2-propanol was decreased to 48percent in 2-methyl-2-propanol containing 4.86percent water.