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Issue 9, 2011
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Understanding the role of carbamate reactivity in fatty acid amide hydrolase inhibition by QM/MM mechanistic modelling

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Abstract

QM/MM modelling of FAAH inactivation by O-biphenyl-3-yl carbamates identifies the deprotonation of Ser241 as the key reaction step, explaining why FAAH is insensitive to the electron-donor effect of conjugated substituents; this may aid design of new inhibitors with improved selectivity and in vivo potency.

Graphical abstract: Understanding the role of carbamate reactivity in fatty acid amide hydrolase inhibition by QM/MM mechanistic modelling

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Publication details

The article was received on 12 Nov 2010, accepted on 21 Dec 2010 and first published on 14 Jan 2011


Article type: Communication
DOI: 10.1039/C0CC04937A
Citation: Chem. Commun., 2011,47, 2517-2519
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    Understanding the role of carbamate reactivity in fatty acid amide hydrolase inhibition by QM/MM mechanistic modelling

    A. Lodola, L. Capoferri, S. Rivara, E. Chudyk, J. Sirirak, E. Dyguda-Kazimierowicz, W. Andrzej Sokalski, M. Mileni, G. Tarzia, D. Piomelli, M. Mor and A. J. Mulholland, Chem. Commun., 2011, 47, 2517
    DOI: 10.1039/C0CC04937A

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