82610-83-1Relevant academic research and scientific papers
Exploitation of subtilisin BPN' as catalyst for the synthesis of peptides containing noncoded amino acids, peptide mimetics and peptide conjugates
Moree, Wilna J.,Sears, Pamela,Kawashiro, Katsuhiro,Witte, Krista,Wong, Chi-Huey
, p. 3942 - 3947 (1997)
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
A new synthesis of protected phosphonodipeptides with an N-terminal amino acid
Sikora, Dorota,Gajda, Tadeusz
, p. 3755 - 3761 (2007/10/03)
A new simple protocol for the direct synthesis of phosphonodipeptides from N-protected amino acids, diethyl 1-azidoalkylphosphonates and tertiary alkyl phosphine (Bu3P, Me3P) was developed. The method is general and the coupling occurred with good yield (42-97%). Depending on the phosphine used and/or mechanism operating during the condensation, the reaction can be accomplished at room temperature, or on heating in toluene. (C) 2000 Elsevier Science Ltd.
UTILISATION DES HYDROLASES EN CHIMIE ORGANIQUE: SYNTHESE DE LIAISONS ESTER ET AMIDE CATALYSEE PAR LA PAPAINE INDUSTRIELLE
Moriniere, Jean-Luc,Danree, Bernard,Guy, Alain
, p. 347 - 358 (2007/10/02)
The use of hydrolases in organic chemistry: synthesis of amide and ester bonds catalyzed by industrial papain.Industrial papain, which is readily available, catalyzed the synthesis of L-Z-alanine ethyl ester (L-ZAEt) in organic medium, under different conditions, with good yields.L-ZAEt was obtained from DL-Z-alanine with 100 percent optical purity.We studied the effects of pH, the solvent/substrate and papain/substrate ratios and the type of organic solvent added, on the L-ZAEt yield.Unreactive D-ZA was also easily isolated from the aqueous phase with good optical purity.This attractive method has been applied to other N-Z-amino acid esters with the same succes.This procedure has been developed for the preparation of peptides using carboxylic or phosphonic substrates.These peptides have anti-bacterial activity. enzymatic catalysis / papain / chymopapain / stereospecific esterification of carboxylic amino acids / dipeptides / phosphonopeptides / anti-bacterial activity
STUDIES ON THE SYNTHESIS OF CHEMOTHERAPEUTICS. PART XIII. SYNTHESIS AND BIOLOGICAL STUDIES ON PHOSPHONOPEPTIDES HAVING ALKYL-, PHENYL-, AND HETEROCYCLIC SUBSTITUENTS.
Kametani, Tetsuji,Suzuki, Yukio,Kigasawa, Kazuo,Hiiragi, Mineharu,Wakisaka, Kikuo,et al.
, p. 295 - 319 (2007/10/02)
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.
