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Issue 69, 2016, Issue in Progress
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Harnessing the pyrroloquinoxaline scaffold for FAAH and MAGL interaction: definition of the structural determinants for enzyme inhibition

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Abstract

This paper describes the development of piperazine and 4-aminopiperidine carboxamides/carbamates supported on a pharmacogenic pyrroloquinoxaline scaffold as inhibitors of the endocannabinoid catabolizing enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL). Structure–activity relationships and molecular modelling studies allowed the definition of the structural requirements for dual FAAH/MAGL inhibition and led to the identification of a small set of derivatives (compounds 5e, i, k, m) displaying a balanced inhibitory profile against both enzymes, with compound 5m being the frontrunner of the subset. Favorable calculated physico-chemical properties suggest further investigation for specific analogues.

Graphical abstract: Harnessing the pyrroloquinoxaline scaffold for FAAH and MAGL interaction: definition of the structural determinants for enzyme inhibition

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Publication details

The article was received on 13 May 2016, accepted on 29 Jun 2016 and first published on 01 Jul 2016


Article type: Paper
DOI: 10.1039/C6RA12524G
Citation: RSC Adv., 2016,6, 64651-64664
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    Harnessing the pyrroloquinoxaline scaffold for FAAH and MAGL interaction: definition of the structural determinants for enzyme inhibition

    M. Brindisi, S. Brogi, S. Maramai, A. Grillo, G. Borrelli, S. Butini, E. Novellino, M. Allarà, A. Ligresti, G. Campiani, V. Di Marzo and S. Gemma, RSC Adv., 2016, 6, 64651
    DOI: 10.1039/C6RA12524G

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