26011-68-7Relevant articles and documents
Thiyl radical-mediated cleavage of allylic C-N bonds: Scope, limitations, and theoretical support to the mechanism
Escoubet, Stephanie,Gastaldi, Stephane,Timokhin, Vitaliy I.,Bertrand, Michele P.,Siri, Didier
, p. 12343 - 12352 (2004)
Thiols mediate the radical isomerization of allylic amines into enamines. The reaction results in the cleavage of the allylic C-N bond, after treatment with aqueous HCI. The mechanism involves the abstraction of an allylic hydrogen α to nitrogen by thiyl
Urethanes synthesis from oxamic acids under electrochemical conditions
Ogbu, Ikechukwu Martin,Lusseau, Jonathan,Kurtay, Gülbin,Robert, Frédéric,Landais, Yannick
, p. 12226 - 12229 (2020/10/26)
Urethane synthesis via oxidative decarboxylation of oxamic acids under mild electrochemical conditions is reported. This simple phosgene-free route to urethanes involves an in situ generation of isocyanates by anodic oxidation of oxamic acids in an alcoholic medium. The reaction is applicable to a wide range of oxamic acids, including chiral ones, and alcohols furnishing the desired urethanes in a one-pot process without the use of a chemical oxidant.
Synthesis of sulfamoylbenzamide derivatives as HBV capsid assembly effector
Sari, Ozkan,Boucle, Sebastien,Cox, Bryan D.,Ozturk, Tugba,Russell, Olivia Ollinger,Bassit, Leda,Amblard, Franck,Schinazi, Raymond F.
, p. 407 - 421 (2017/07/10)
The synthesis of novel series of sulfamoylbenzamides as HBV capsid assembly effector is reported. The structure was divided into five parts which were independently modified as part of our lead optimization. All synthesized compounds were evaluated for their anti-HBV activity and toxicity in human hepatocytes, lymphocytes and other cells. Additionally, we assessed their effect on HBV cccDNA formation in an HBeAg reporter cell-based assay. Among the 27 compounds reported, several analogs exhibited submicromolar activities and significant reduction of HBeAg secretion. Selected compounds were studied under negative-stain electron microscopy for their ability to disrupt the HBV capsid formation. Structures were modeled into a binding site recently identified in the HBV capsid protein for similar molecules to rationalize the structure-activity relationships for this family of compounds.