69193-11-9

Basic information

• Product Name: Z-L-Phe-L-Val-NH₂
• Synonyms: Z-L-Phe-L-Val-NH₂
• CAS NO: 69193-11-9
• Molecular Weight: 397.474
• Mol File: 69193-11-9.mol

Chemical Properties

• CAS DataBase Reference: Z-L-Phe-L-Val-NH₂(CAS DataBase Reference)
• NIST Chemistry Reference: Z-L-Phe-L-Val-NH₂(69193-11-9)
• EPA Substance Registry System: Z-L-Phe-L-Val-NH₂(69193-11-9)

Safety Data

• Hazardous Substances Data: 69193-11-9(Hazardous Substances Data)

Upstream product

• 4540-60-7 L-valinamide 
• 3272-95-5 Z-L-Phe p-chlorophenyl ester 
• 1161-13-3 N-Cbz-L-Phe 
• 3014-80-0 (S)-2-amino-3-methylbutanamide hydrochloride 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 126028-14-6 2,2,2-trifluoroethyl ((benzyloxy)carbonyl)-L-phenylalaninate 
• 13123-00-7 (2S)-2-[((2S)-2-{[(benzyloxy)carbonyl]amino}-3-phenylpropanoyl)amino]-3-methylbutanoic acid 
• 130457-37-3 [1-(1-Cyano-2-methyl-propylcarbamoyl)-2-phenyl-ethyl]-carbamic acid benzyl ester 
• 125453-25-0 [1-(1-Benzotriazol-1-yl-2-methyl-propylcarbamoyl)-2-phenyl-ethyl]-carbamic acid benzyl ester 
• 4816-89-1 Cbz-Phe-OCH₂CONH₂ 

Downstream Products

• 130457-28-2 1-<1-(N-benzyloxycarbonyl-phenylalanyl-valylamino)-3-methylbutyl>benzotriazole 
• 127536-32-7 {(R)-1-[(R)-1-((S)-1-Cyano-3-methyl-butylcarbamoyl)-2-methyl-propylcarbamoyl]-2-phenyl-ethyl}-carbamic acid benzyl ester 
• 127536-33-8 N-benzyloxycarbonyl-L-phenylalanyl-L-valyl-D,L-leucine amide 
• 164861-48-7 Z-L-Phe-L-Val-L-Pro-NH₂ 
• 72-18-4 L-valine 
• 63-91-2 L-phenylalanine 

Relevant articles and documents

Kinetically controlled peptide synthesis mediated by papain using the carbamoylmethyl ester as an acyl donor

A series of dipeptides were synthesized generally in good yields with carbamoylmethyl (Cam) esters as acyl donors in the presence of a cysteine protease, papain, immobilized on Celite. Several segment condensations were also achieved generally in high yields without danger of racemization and formation of the secondary-hydrolysis product. Moreover, partial sequences of some bioactive peptides were prepared through segment condensations, and aimed-at peptides were obtained generally in high yields without the racemization of C-terminal residues of the carboxyl components. Thus, the superiority of the Cam ester in the kinetically controlled peptide synthesis was once again ascertained in couplings mediated by the cysteine protease as in those catalyzed by the serine proteases reported earlier.

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.

Pronase catalysed peptide syntheses

A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.

α-Chymotrypsin-catalysed peptide synthesis using activated esters as acyl donors

The coupling efficiency in α-chymotrypsin-catalysed peptide synthesis is greatly improved by the use of activated esters such as the 2,2,2-trifluoroethyl ester as acyl donor instead of the conventional methyl ester; this approach is useful for the incorporation of non-protein amino acids into peptides.

Benzotriazole-assisted Synthesis of α-Acylaminonitriles and a Conceptually Novel Method for Peptide Elongation

A general method for the synthesis of α-acylamino nitriles is reported.Initially, the adducts resulting from Mannich-type condensation of benzotriazole with an aldehyde and an amide are prepared.These undergo elimination of benzotriazole with cyanide to g

Model Studies on Carboxypeptidase Y Catalyzed Peptide Synthesis in an Aqueous-Organic Two-Phase System

Carboxypeptidase Y catalyzes in a biphasic system containing carbon tetrachloride and carbonate buffer the reaction of Z-Phe-OMe and various Z- and Boc-protected dipeptide methyl esters with Val-NH2 and Leu-NH2 respectively.This method has been applied to