87967-38-2Relevant academic research and scientific papers
Copper-catalyzed: N -(hetero)arylation of amino acids in water
Sharma, Krishna K.,Mandloi, Meenakshi,Rai, Neha,Jain, Rahul
, p. 96762 - 96767 (2016/10/24)
An environmentally benign, mild, cost-effective and gram-scalable copper-catalyzed method for the N-(hetero)arylation of zwitterionic natural and unnatural amino acids using 2-isobutyrylcyclohexanone as a β-diketone ligand and aryl bromides as coupling partners in water for 50 min at 90 °C under microwave irradiation is reported. Electronically and sterically diverse aryl coupling partners were inserted efficiently, including challenging heteroaryl electrophilic partners in high yields without affecting the enantiopurity of the product.
Dual Bronsted acid/nucleophilic activation of carbonylimidazole derivatives
Heller, Stephen T.,Fu, Tingting,Sarpong, Richmond
supporting information; experimental part, p. 1970 - 1973 (2012/06/01)
Carbonylimidazole derivatives have been found to be highly active acylation reagents for esterification and amidation in the presence of pyridinium salts. These reactions are thought to involve both Bronsted acid and nucleophilic catalysis. This mode of activation has been applied to the synthesis of difficult to access oxazolidinones, as well as esters and amides. Finally, the use of pyridinium salts has been shown to accelerate the esterification of carboxylic acids with imidazole carbamates.
A cyclohexanecarboxamide derivative with inhibitory effects on Schistosoma mansoni cercarial serine protease and penetration of mice skin by the parasite
Bahgat, Mahmoud,Aboul-Enein, Mohamed N.,El Azzouny, Aida A.,Maghraby, Amany,Ruppel, Andreas,Soliman, Wael M.
scheme or table, p. 333 - 340 (2009/12/24)
A cyclohexanecarboxamide derivative, N-phenyl-N-[1-(piperidine-1-carbonyl) cyclohexyl] benzamide (MNRC-5), was evaluated for its inhibitory effects on Schistosoma mansoni cercarial serine protease activity and cercarial penetration. MNRC-5 exerted an inhi
Potent and selective cathepsin K inhibitors
Shinozuka, Tsuyoshi,Shimada, Kousei,Matsui, Satoshi,Yamane, Takahiro,Ama, Mayumi,Fukuda, Takeshi,Taki, Motohiko,Takeda, Yuko,Otsuka, Eri,Yamato, Michiko,Mochizuki, Shin-ichi,Ohhata, Keiko,Naito, Satoru
, p. 6789 - 6806 (2007/10/03)
A novel series of cathepsin K inhibitors derived from Novartis compound I is described. Optimization of the P1, P3, and P1′ units led to the identification of 4-aminophenoxyacetic acid 24b with an IC50 value of 4.8 nM, which possessed an excell
4-Aminophenoxyacetic acids as a novel class of reversible cathepsin K inhibitors
Shinozuka, Tsuyoshi,Shimada, Kousei,Matsui, Satoshi,Yamane, Takahiro,Ama, Mayumi,Fukuda, Takeshi,Taki, Motohiko,Naito, Satoru
, p. 1502 - 1505 (2007/10/03)
We have designed and synthesized a novel series of 3-biphenylamino acid amides as cathepsin K inhibitors based on compound I. In these inhibitors, we have discovered 4-aminophenoxyacetic acids 43 and 47 with good IC50 values, although lipophili
