Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling

Lodola, Alessio, Mor, Marco, Rivara, Silvia, Christov, Christo, Tarzia, Giorgio, Piomelli, Daniele and Mulholland, Adrian (2008) Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling. Chemical Communications, 2008 (2). pp. 214-216. ISSN 1359-7345

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Official URL: http://dx.doi.org/10.1039/b714136j

Abstract

Modelling of the mechanism of covalent adduct formation by the inhibitor O-arylcarbamate URB524 in FAAH shows that only one of the two possible inhibitor binding orientations is consistent with the experimentally observed irreversible carbamoylation of the nucleophile serine: this is a potentially crucial insight for designing new covalent inhibitors of this promising drug target.

Item Type: Article
Uncontrolled Keywords: Fatty acids, Inhibitors, Chemical
Subjects: F100 Chemistry
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: EPrints Services
Date Deposited: 18 Feb 2011 10:51
Last Modified: 10 Aug 2015 11:46
URI: http://nrl.northumbria.ac.uk/id/eprint/3207

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