Issue 9, 2011

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

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

Supplementary files

Article information

Article type
Communication
Submitted
12 Nov 2010
Accepted
21 Dec 2010
First published
14 Jan 2011

Chem. Commun., 2011,47, 2517-2519

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements