52386-79-5Relevant academic research and scientific papers
Synthesis and biological evaluation of N-mercaptoacylcysteine derivatives as leukotriene A4 hydrolase inhibitors
Enomoto, Hiroshi,Morikawa, Yuko,Miyake, Yurika,Tsuji, Fumio,Mizuchi, Maki,Suhara, Hiroshi,Fujimura, Ken-ichi,Horiuchi, Masato,Ban, Masakazu
scheme or table, p. 442 - 446 (2011/02/26)
We studied synthetic modifications of N-mercaptoacylamino acid derivatives to develop a new class of leukotriene A4 (LTA4) hydrolase inhibitors. S-(4-Dimethylamino)benzyl-l-cysteine derivative 2a (SA6541) showed inhibitory activity against LTA4 hydrolase (IC50, 270 nM) and selectivity over other metallopeptidases except angiotensin-converting enzyme (ACE, IC50, 520 nM). Modification at the para-substituent of the phenyl ring of compound 2a improved LTA4 hydrolase inhibitory activity as well as selectivity over ACE. Finally, we obtained S-(4-cyclohexyl)benzy-l-cysteine derivatives 11l and 16i as potent and selective LTA4 hydrolase inhibitors.
Isozyme-specific glutathione-S-transferase inhibitors: Design and synthesis
Lyttle,Hocker,Hui,Caldwell,Aaron,Engqvist- Goldstein,Flatgaard,Bauer
, p. 189 - 194 (2007/10/02)
Glutathione-S-transferase (GST) isozyme-selective inhibitors were designed by an empirically guided strategy. In the first phase, literature data were used to select C-terminal modifications which generated maximum variation in the catalytic efficiency (V
