130766-04-0Relevant articles and documents
Ecological base-conditioned preparation of dipeptides using unprotected α-amino acids containing hydrophilic side chains
Ezawa, Tetsuya,Jung, Seunghee,Kawashima, Yuya,Noguchi, Takuya,Imai, Nobuyuki
, p. 689 - 696 (2017/07/22)
The coupling reactions of 3-phenylpropanoic acid and Ncarboxybenzyl á-amino acids with unprotected á-amino acids containing hydrophilic side chains such as aliphatic alcohol, aromatic alcohol, thiol, carboxylic acid, and amide afforded the corresponding amides in 6696% yield without racemization via the corresponding mixed carbonic carboxylic anhydrides under basic conditions through an ecological green synthetic method.
Convenient peptide synthesis using unprotected α-amino acids containing another hydrophilic moiety under basic conditions
Noguchi, Takuya,Jung, Seunghee,Imai, Nobuyuki
scheme or table, p. 577 - 579 (2012/08/08)
Carboxylic acids 1 and 7 reacted effectively with unprotected α-amino acids 2 containing another hydrophilic moiety under basic conditions via activation by ethyl chloroformate and triethylamine to afford the corresponding amides in 7499% yields.
Synthesis and structure - Activity relationships of N -(2-Oxo-3-oxetanyl) amides as N -acylethanolamine-hydrolyzing acid amidase inhibitors
Solorzano, Carlos,Antonietti, Francesca,Duranti, Andrea,Tontini, Andrea,Rivara, Silvia,Lodola, Alessio,Vacondio, Federica,Tarzia, Giorgio,Piomelli, Daniele,Mor, Marco
experimental part, p. 5770 - 5781 (2010/10/20)
The fatty acid ethanolamides (FAEs) are a family of bioactive lipid mediators that include the endogenous agonist of peroxisome proliferator- activated receptor-α, palmitoylethanolamide (PEA). FAEs are hydrolyzed intracellularly by either fatty acid amide hydrolase or N-acylethanolamine- hydrolyzing acid amidase (NAAA). Selective inhibition of NAAA by (S)-N-(2-oxo-3-oxetanyl)-3-phenylpropionamide [(S)-OOPP, 7a] prevents PEA degradation in mouse leukocytes and attenuates responses to proinflammatory stimuli. Starting from the structure of 7a, a series of β-lactones was prepared and tested on recombinant rat NAAA to explore structure-activity relationships (SARs) for this class of inhibitors and improve their in vitro potency. Following the hypothesis that these compounds inhibit NAAA by acylation of the catalytic cysteine, we identified several requirements for recognition at the active site and obtained new potent inhibitors. In particular, (S)-N-(2-oxo-3-oxetanyl)biphenyl-4-carboxamide (7h) was more potent than 7a at inhibiting recombinant rat NAAA activity (7a, IC50 = 420 nM; 7h, IC50 = 115 nM) in vitro and at reducing carrageenan-induced leukocyte infiltration in vivo.
