Thiadiazolopiperazinyl ureas as inhibitors of fatty acid amide hydrolase.
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 presented.
Keith
John M
JM
Johnson & Johnson Pharmaceutical Research and Development, LLC, 3210 Merryfield Row, San Diego, CA 92121, USA.
Apodaca
Richard
R
Xiao
Wei
W
Seierstad
Mark
M
Pattabiraman
Kanaka
K
Wu
Jiejun
J
Webb
Michael
M
Karbarz
Mark J
MJ
Brown
Sean
S
Wilson
Sandy
S
Scott
Brian
B
Tham
Chui-Se
CS
Luo
Lin
L
Palmer
James
J
Wennerholm
Michelle
M
Chaplan
Sandra
S
Breitenbucher
J Guy
JG
D000581:Amidohydrolases / Q000037:antagonists & inhibitors* / Q000172:deficiency / Q000235:genetics; D000818:Animals; D051379:Mice; D018345:Mice, Knockout; D010879:Piperazines / Q000737:chemistry / Q000493:pharmacokinetics / Q000494:pharmacology*; D013830:Thiadiazoles / Q000737:chemistry / Q000493:pharmacokinetics / Q000494:pharmacology*; D014508:Urea / Q000031:analogs & derivatives* / Q000737:chemistry / Q000493:pharmacokinetics / Q000494:pharmacology*; D000099252:Fatty Acid Amide Hydrolases
D000581:Amidohydrolases; D010879:Piperazines; D013830:Thiadiazoles; D014508:Urea; D000099252:Fatty Acid Amide Hydrolases