Background:

JNJ-1661010, a piperazinyl phenyl urea with its structure distinct from alkylcarbamic acid esters and α–ketoheterocyclic compounds, is a potent and selective inhibitor of fatty acid amide hydrolase (FAAH) that covalently binds to the active site of FAAH through cleavage of the urea functionality generating aniline and a FAAH-poperazinyl carbamate. The inhibition of JNJ-1661010 against FAAH is reversible through the hydrolysis of the carbamate leading to the release of the piperazinyl fragment and the restoration of enzymatic functionality of FAAH. According to results of previous studies, JNJ-1661010 displays its inhibition against recombinant FAAH with values of 50% inhibition concentration IC₅₀of 10 nM and 12 nM in rat and human respectively.

Reference

[1].Karbarz MJ, Luo L, Chang L, Tham CS, Palmer JA, Wilson SJ, Wennerholm ML, Brown SM, Scott BP, Apodaca RL, Keith JM, Wu J, Breitenbucher JG, Chaplan SR, Webb M. Biochemical and biological properties of 4-(3-phenyl-[1,2,4] thiadiazol-5-yl)-piperazine-1-carboxylic acid phenylamide, a mechanism-based inhibitor of fatty acid amide hydrolase. Anesth Analg. 2009;108(1):316-329.