Discovery of potent, non-carbonyl inhibitors of fatty acid amide hydrolase (FAAH)

Sumithra Gowlugari; Jeff DeFalco; Margaret T. Nguyen; Carl Kaub; Candace Chi; Matthew A. J. Duncton; Daniel E. Emerling; Michael G. Kelly; John Kincaid; Fabien Vincent

doi:10.1039/C2MD20146A

Discovery of potent, non-carbonyl inhibitors of fatty acid amide hydrolase (FAAH)†

Sumithra Gowlugari,^a Jeff DeFalco,^a Margaret T. Nguyen,^a Carl Kaub,^a Candace Chi,^a Matthew A. J. Duncton,^a Daniel E. Emerling,^a Michael G. Kelly,^a John Kincaid^a and Fabien Vincent ‡*^a

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^a Renovis, Inc. (a wholly-owned subsidiary of Evotec AG), Two Corporate Drive, South San Francisco, USA
E-mail: fabien_vincent_us@yahoo.com

Abstract

Fatty acid amide hydrolase (FAAH) inhibition is a promising target for the treatment of pain, anxiety and depression. The vast majority of FAAH inhibitors contain an electrophilic moiety and are known to react covalently with the enzyme. Herein we present the discovery of potent inhibitors, such as RN-450 29, which are based upon a novel tetrahydropyridopyridine scaffold lacking an obvious electrophilic site, and which appear to inhibit FAAH in a reversible and non-covalent manner.

MedChemComm

Discovery of potent, non-carbonyl inhibitors of fatty acid amide hydrolase (FAAH)†

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Discovery of potent, non-carbonyl inhibitors of fatty acid amide hydrolase (FAAH)

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