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

Alessio Lodola, Marco Mor, Silvia Rivara, Christo Christov, Giorgio Tarzia, Daniele Piomelli, Adrian Mulholland

Research output: Contribution to journalArticlepeer-review

56 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)214-216
JournalChemical Communications
Volume2008
Issue number2
DOIs
Publication statusPublished - 2008

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