14303-96-9Relevant articles and documents
Aminolysis of carboxylic acid esters in direct, bicontinual, and inverse microemulsions based on cetyltrimethylammonium bromide
Mirgorodskaya,Kudryavtseva,Shtykova,Bogomolova,Shtykov
, p. 1108 - 1112 (2005)
The reactivity of primary alkylamines in cleavage of p-nitrophenyl esters of carboxylic acids in microemulsions of different structures based on cetyltrimethylammonium bromide was studied. The aminolysis rate considerably increases in going from inverse to direct microemulsions, mainly owing to the concentration of the reactants in the boundary layer. 2005 Pleiades Publishing, Inc.
Environmentally benign decarboxylative: N-, O-, and S-Acetylations and acylations
Ghosh, Santanu,Purkait, Anisha,Jana, Chandan K.
supporting information, p. 8721 - 8727 (2020/12/30)
An operationally simple and general method for acetylation and acylation of a wide variety of substrates (amines, alcohols, phenols, thiols, and hydrazones) has been reported. Meldrum's acid and its derivatives have been used as an air-stable, non-volatile, cost-effective, and easy to handle acetylating/acylating agent. Easily separable byproducts (CO2 and acetone) allowed the isolation of analytically pure acetylated products without the requirement of work-up and any chromatography. This journal is
Bis(dialkylaminethiocarbonyl)disulfides as potent and selective monoglyceride lipase inhibitors
Kapanda, Coco N.,Muccioli, Giulio G.,Labar, Geoffray,Poupaert, Jacques H.,Lambert, Didier M.
supporting information; experimental part, p. 7310 - 7314 (2010/07/14)
Monoglyceride lipase (MGL) inhibition may offer an approach in treating diseases in which higher 2-arachidonoyglycerol activity would be beneficial. We report here the synthesis and pharmacological evaluation of bis(dialkylaminethiocarbonyl)disulfide derivatives as irreversible MGL inhibitors. Inhibition occurs through interactions with MGL C208 and C242 residues, and these derivatives exhibit high inhibition selectivity over fatty acid amide hydrolase, another endocannabinoid-hydrolyzing enzyme. 2009 American Chemical Society.
