17187-05-2

Basic information

• Product Name: Z-PHE-GLY-NH2
• Synonyms: Z-PHE-GLY-NH2
• CAS NO: 17187-05-2
• Molecular Formula: C₁₉H₂₁N₃O₄
• Molecular Weight: 355.39
• Mol File: 17187-05-2.mol
• Article Data: 11

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-PHE-GLY-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PHE-GLY-NH2(17187-05-2)
• EPA Substance Registry System: Z-PHE-GLY-NH2(17187-05-2)

Safety Data

• Hazardous Substances Data: 17187-05-2(Hazardous Substances Data)

Upstream product

• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 598-41-4 H-Gly-NH₂ 
• 3272-95-5 Z-L-Phe p-chlorophenyl ester 
• 4816-89-1 Cbz-Phe-OCH₂CONH₂ 
• 1668-10-6 glycinamide hydrochloride 
• 1161-13-3 N-Cbz-L-Phe 
• 60379-01-3 N-(benzyloxycarbonyl)-L-phenylalanine benzyl ester 
• 126028-14-6 2,2,2-trifluoroethyl ((benzyloxy)carbonyl)-L-phenylalaninate 
• 52641-32-4 N-benzyloxycarbonyl-L-phenylalanyl chloride 

Downstream Products

• 5184-17-8 N-benzyloxycarbonyl-L-phenylalanylglycine methyl ester 
• 38678-61-4 H-L-Phe-Gly-NH₂ 

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.

Synthesis and biological evaluation of analogues of the antibiotic pantocin B

Strains of the bacteria Erwinia herbicola produce antibiotics that effectively control E. amylovora, the bacterial pathogen responsible for the plant disease fire blight. Pantocin B was the first of these antibiotics to be characterized, and a flexible sy

Expanded structural and stereospecificity in peptide synthesis with chemically modified mutants of subtilisin

Employing the strategy of combined site directed mutagenesis and chemical modification, we previously generated chemically modified mutant enzymes (CMMs) of subtilisin Bacillus lentus (SBL). We now report the use of these SBL-CMMs for peptide coupling rea