1062512-81-5Relevant articles and documents
Heteroaryl urea inhibitors of fatty acid amide hydrolase: Structure-mutagenicity relationships for arylamine metabolites
Tichenor, Mark S.,Keith, John M.,Jones, William M.,Pierce, Joan M.,Merit, Jeff,Hawryluk, Natalie,Seierstad, Mark,Palmer, James A.,Webb, Michael,Karbarz, Mark J.,Wilson, Sandy J.,Wennerholm, Michelle L.,Woestenborghs, Filip,Beerens, Dominiek,Luo, Lin,Brown, Sean M.,Boeck, Marlies De,Chaplan, Sandra R.,Breitenbucher, J. Guy
, p. 7357 - 7362 (2013/02/21)
The structure-activity relationships for a series of heteroaryl urea inhibitors of fatty acid amide hydrolase (FAAH) are described. Members of this class of inhibitors have been shown to inactivate FAAH by covalent modification of an active site serine with subsequent release of an aromatic amine from the urea electrophile. Systematic Ames II testing guided the optimization of urea substituents by defining the structure-mutagenicity relationships for the released aromatic amine metabolites. Potent FAAH inhibitors were identified having heteroaryl amine leaving groups that were non-mutagenic in the Ames II assay.
Thiadiazolopiperazinyl ureas as inhibitors of fatty acid amide hydrolase
Keith, John M.,Apodaca, Richard,Xiao, Wei,Seierstad, Mark,Pattabiraman, Kanaka,Wu, Jiejun,Webb, Michael,Karbarz, Mark J.,Brown, Sean,Wilson, Sandy,Scott, Brian,Tham, Chui-Se,Luo, Lin,Palmer, James,Wennerholm, Michelle,Chaplan, Sandra,Breitenbucher, J. Guy
scheme or table, p. 4838 - 4843 (2009/05/07)
A series of thiadiazolopiperazinyl aryl urea fatty acid amide hydrolase (FAAH) inhibitors is described. The molecules were found to inhibit the enzyme by acting as mechanism-based substrates, forming a covalent bond with Ser241. SAR and PK properties are
