17425-24-0Relevant articles and documents
A new one-pot synthesis of thiocarbamates from isocyanates and disulfides in the presence of Zn/AlCl3 system
Movassagh, Barahman,Zakinezhad, Yousef
, p. 1330 - 1331 (2005)
A novel method has been developed for the synthesis of S-alkyl(aryl) thiocarbamates. The route involves, first, the formation of zinc thiolates by reductive cleavage of disulfides in the presence of Zn/AlCl3 system; then subsequent reaction of
A selenium-catalysed synthesis of thiocarbamates from nitroarenes, carbon monoxide and thiols under mild conditions
Zhang, Xiao-Peng,Lu, Shi-Wei
experimental part, p. 589 - 591 (2009/08/15)
An improved method for the selenium-catalysed synthesis of thiocarbamates under mild conditions has been developed. With acetone as solvent, the one-pot selenium-catalysed carbonylation of nitroarenes and thiols with carbon monoxide proceeds smoothly at atmospheric pressure and ambient temperature.
Potent inhibitory effects of N-aryl S-alkylthiocarbamate derivatives on the dopa oxidase activity of mushroom tyrosinase
Lee, Kun Ho,Koketsu, Mamoru,Choi, Sang Yoon,Lee, Kang Jin,Lee, Pyeongjae,Ishihara, Hideharu,Kim, Sun Yeou
, p. 747 - 749 (2007/10/03)
This study reports the potent inhibitory effect of N-aryl S-alkylthiocarbamate derivatives on mushroom tyrosinase (MT) activity. N-Aryl S-alkylthiocarbamate derivatives were found to exhibit a potent inhibitory effect on the dopa (3,4-dihydroxyphenylalanine) oxidase activity of mushroom tyrosinase. Most of the N-aryl S-alkylthiocarbamate derivatives (compounds from A to J) exhibited higher inhibitory effects than kojic acid (IC50=318 μm), a well known tyrosinase inhibitor. Tyrosinase was the most inhibited by S-phenetyl N-phenylthiocarbamate (compound E, IC50=7.25 μM), and this inhibition was 44 times stronger than that of kojic acid. Compound E exhibited 95.0% of inhibition at 100 μM. A kinetic study of MT inhibition by compound E using the Lineweaver-Burk plots analysis was performed. And the kinetics profiles observed suggest that compound E competitively inhibits MT.