65118-54-9

Basic information

• Product Name: Z-PHE-ALA-NH2
• Synonyms: Z-PHE-ALA-NH2
• CAS NO: 65118-54-9
• Molecular Formula: C₂₀H₂₃N₃O₄
• Molecular Weight: 369.41
• Mol File: 65118-54-9.mol
• Article Data: 8

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-PHE-ALA-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PHE-ALA-NH2(65118-54-9)
• EPA Substance Registry System: Z-PHE-ALA-NH2(65118-54-9)

Safety Data

• Hazardous Substances Data: 65118-54-9(Hazardous Substances Data)

Upstream product

• 3338-39-4 N-benzyloxycarbonyl-L-phenylalanyl-L-alanine 
• 1161-13-3 N-Cbz-L-Phe 
• 7324-05-2 L-alanine amide 
• 4816-89-1 Cbz-Phe-OCH₂CONH₂ 
• 60379-01-3 N-(benzyloxycarbonyl)-L-phenylalanine benzyl ester 
• 33208-99-0 (S)-alaninamide hydrochloride 
• 28944-94-7 (S)-methyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)propanoate 

Downstream Products

• 1043922-58-2 N-(benzyloxycarbonyl)phenylalanyl-alanine nitrile 
• 3338-39-4 N-benzyloxycarbonyl-L-phenylalanyl-L-alanine 
• 28944-94-7 (S)-methyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)propanoate 
• 7324-05-2 L-alanine amide 
• 63-91-2 L-phenylalanine 

Relevant articles and documents

Convenient primary amidation of N-protected phenylglycine and dipeptides without racemization or epimerization

Primary amidation of N-protected phenylglycine and dipeptide proceeded easily to afford the corresponding amides in 57-95% yields with 99% ee and 81-99% de, respectively. The procedure is very easy to avoid racemization and epimerization of the products in the reactions by keeping exactly the reaction temperature at -15 C when the activation of carboxylic acids, followed by the reaction of the mixed carbonic carboxylic anhydride with NH4Cl.

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.

Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis

Site-selective glycosylation at position 166 at the base of the primary specificity S1 pocket in the serine protease subtilisin Bacillus lentus (SBL) created glycoproteins that are capable of catalyzing the coupling reactions of not only L- ami