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@ARTICLE{Palermo:829382,
author = {Palermo, Giulia and Favia, Angelo D. and Convertino, Marino
and De Vivo, Marco},
title = {{T}he {M}olecular {B}asis for {D}ual {F}atty {A}cid {A}mide
{H}ydrolase ({FAAH})/{C}yclooxygenase ({COX}) {I}nhibition},
journal = {ChemMedChem},
volume = {11},
number = {12},
issn = {1860-7179},
address = {Weinheim [u.a.]},
publisher = {Wiley-VCH},
reportid = {FZJ-2017-03095},
pages = {1252 - 1258},
year = {2016},
abstract = {The design of multitarget-directed ligands is a promising
strategy for discovering innovative drugs. Here, we report a
mechanistic study that clarifies key aspects of the dual
inhibition of the fatty acid amide hydrolase (FAAH) and the
cyclooxygenase (COX) enzymes by a new multitarget-directed
ligand named ARN2508
(2-[3-fluoro-4-[3-(hexylcarbamoyloxy)phenyl]phenyl]propanoic
acid). This potent dual inhibitor combines, in a single
scaffold, the pharmacophoric elements often needed to block
FAAH and COX, that is, a carbamate moiety and the
2-arylpropionic acid functionality, respectively. Molecular
modeling and molecular dynamics simulations suggest that
ARN2508 uses a noncovalent mechanism of inhibition to block
COXs, while inhibiting FAAH via the acetylation of the
catalytic Ser241, in line with previous experimental
evidence for covalent FAAH inhibition. This study proposes
the molecular basis for the dual FAAH/COX inhibition by this
novel hybrid scaffold, stimulating further experimental
studies and offering new insights for the rational design of
novel anti-inflammatory agents that simultaneously act on
FAAH and COX.},
cin = {IAS-5 / INM-9},
ddc = {540},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
pnm = {899 - ohne Topic (POF3-899)},
pid = {G:(DE-HGF)POF3-899},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000380024300008},
pubmed = {pmid:26593700},
doi = {10.1002/cmdc.201500507},
url = {https://juser.fz-juelich.de/record/829382},
}