82610-83-1

Basic information

• Product Name: ester ethylique de l'acide (N-benzyloxycarbonyl)-L-phenylalanyl-aminomethylphosphonique
• Synonyms: ester ethylique de l'acide (N-benzyloxycarbonyl)-L-phenylalanyl-aminomethylphosphonique
• CAS NO: 82610-83-1
• Molecular Weight: 448.456
• Mol File: 82610-83-1.mol
• Article Data: 5

Chemical Properties

• CAS DataBase Reference: ester ethylique de l'acide (N-benzyloxycarbonyl)-L-phenylalanyl-aminomethylphosphonique(CAS DataBase Reference)
• NIST Chemistry Reference: ester ethylique de l'acide (N-benzyloxycarbonyl)-L-phenylalanyl-aminomethylphosphonique(82610-83-1)
• EPA Substance Registry System: ester ethylique de l'acide (N-benzyloxycarbonyl)-L-phenylalanyl-aminomethylphosphonique(82610-83-1)

Safety Data

• Hazardous Substances Data: 82610-83-1(Hazardous Substances Data)

Upstream product

• 50917-72-1 aminomethylphosphonic acid diethyl ester 
• 60379-01-3 N-(benzyloxycarbonyl)-L-phenylalanine benzyl ester 
• 33512-26-4 diethyl (phthalimidomethyl)phosphonate 
• 17982-55-7 diethyl (azidomethyl)phosphonate 
• 1161-13-3 N-Cbz-L-Phe 
• 3588-57-6 Z-DL-Phe-OH 
• 41518-17-6 Z-Phe-O-COO-isoBu 

Downstream Products

• 60668-15-7 acide L-phenylalanyl-aminomethylphosphonique 

Relevant articles and documents

Exploitation of subtilisin BPN' as catalyst for the synthesis of peptides containing noncoded amino acids, peptide mimetics and peptide conjugates

The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts nume

SYNTHESIS OF PHOSPHONOPEPTIDES WITH THE USE OF PIVALOYL CHLORIDE

-

STUDIES ON THE SYNTHESIS OF CHEMOTHERAPEUTICS. PART XIII. SYNTHESIS AND BIOLOGICAL STUDIES ON PHOSPHONOPEPTIDES HAVING ALKYL-, PHENYL-, AND HETEROCYCLIC SUBSTITUENTS.

New antibacterial phosphonopeptides (3) were synthesized in order to improve the stability against hydrolysis by peptidase and the antibacterial spectra.Synthesis of them was accomplished by condensation of the N-carbobenzoxyamino acid with diethyl aminoalkylphosphonate followed by deprotection and hydrolysis.The antibacterial activity was evaluated in a defined medium and the stability against hydrolysis by rat liver homogenates was examined.Chemical modification of the N-terminal amino acid moiety of the phosphonopeptide containing sulfur or oxygen atom at β- or γ-position of the N-terminal α-amino acid residue lost rapidly their in vivo activity in spite of the high in vitro activity.The para substituted phenylalanyl-1-aminoethyl-phosphonic acids showed higher stability and slightly lower activity compared with those of the corresponding ortho- and meta-substituted isomers.Some of these para-substituted compounds (e.g. 9β, 10β, and 19β) exhibited the same level of the biological activity as that of Alafosfalin (1) in potency of the activity, broadness of the spectrum, and the serum level in mice after peroral administration.Phosphonopeptides consisted of unnatural amino acids and aminomethylphosphonic acid showed generally the extended spectra and activities, but these compounds were very fragile to hydrolysis by peptidase.None of phosphonopeptides containing 2-aminoethylphosphonic acid had the activity.