Design, Synthesis, and In Vitro Evaluation of Carbamate Derivatives of 2-Benzoxazolyl- and 2-Benzothiazolyl-(3-hydroxyphenyl)-methanones as Novel Fatty Acid Amide Hydrolase Inhibitors

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Myllymäki, Mikko J.
dc.contributor.author Saario, Susanna M.
dc.contributor.author Kataja, Antti O.
dc.contributor.author Castillo-Melendez, Joel A.
dc.contributor.author Nevalainen, Tapio
dc.contributor.author Juvonen, Risto O.
dc.contributor.author Järvinen, Tomi
dc.contributor.author Koskinen, Ari M.P.
dc.date.accessioned 2016-09-23T09:31:52Z
dc.date.issued 2007
dc.identifier.citation Myllymäki , M J , Saario , S M , Kataja , A O , Castillo-Melendez , J A , Nevalainen , T , Juvonen , R O , Järvinen , T & Koskinen , A M P 2007 , ' Design, Synthesis, and In Vitro Evaluation of Carbamate Derivatives of 2-Benzoxazolyl- and 2-Benzothiazolyl-(3-hydroxyphenyl)-methanones as Novel Fatty Acid Amide Hydrolase Inhibitors ' JOURNAL OF MEDICINAL CHEMISTRY , vol 50 , no. 17 , pp. 4236-4242 . DOI: 10.1021/jm070501w en
dc.identifier.issn 0022-2623
dc.identifier.issn 1520-4804
dc.identifier.other PURE UUID: f4db7348-c42a-4ca1-9199-e00df6e2728f
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/design-synthesis-and-in-vitro-evaluation-of-carbamate-derivatives-of-2benzoxazolyl-and-2benzothiazolyl3hydroxyphenylmethanones-as-novel-fatty-acid-amide-hydrolase-inhibitors(f4db7348-c42a-4ca1-9199-e00df6e2728f).html
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/7159733/ms132.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/22490
dc.description.abstract Fatty acid amide hydrolase (FAAH) is an intracellular serine hydrolase, which catalyzes the hydrolysis of the endocannabinoid N-arachidonoylethanolamide to arachidonic acid and ethanolamine. FAAH also hydrolyzes another endocannabinoid, 2-arachidonoylglycerol (2-AG). However, 2-AG has been assumed to be hydrolyzed mainly by monoacylglycerol lipase (MAGL) or a MAGL-like enzyme. Inhibition of FAAH or MAGL activity might lead to beneficial effects in many physiological disorders such as pain, inflammation, and anxiety due to increased endocannabinoid-induced activation of cannabinoid receptors CB1 and CB2. In the present study, a total of 34 novel compounds were designed, synthesized, characterized, and tested against FAAH and MAGL-like enzyme activity. Altogether, 16 compounds were found to inhibit FAAH with half-maximal inhibition concentrations (IC50) between 28 and 380 nM. All the active compounds belong to the structural family of carbamates. Compounds 14 and 18 were found to be the most potent FAAH inhibitors, which may serve as lead structures for novel FAAH inhibitors. en
dc.format.extent 4236-4242
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries JOURNAL OF MEDICINAL CHEMISTRY en
dc.relation.ispartofseries Volume 50, issue 17 en
dc.rights openAccess en
dc.title Design, Synthesis, and In Vitro Evaluation of Carbamate Derivatives of 2-Benzoxazolyl- and 2-Benzothiazolyl-(3-hydroxyphenyl)-methanones as Novel Fatty Acid Amide Hydrolase Inhibitors en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department School services, CHEM
dc.contributor.department Department of Chemistry en
dc.subject.keyword 2-Arachidonoylglycerol (2-AG)
dc.subject.keyword central nervous system
dc.subject.keyword enzyme inhibitor
dc.subject.keyword fatty acid amide hydrolase (FAAH)
dc.subject.keyword monoacylglycerol lipase (MAGL)
dc.subject.keyword N-Arachidonoylethanolamine (AEA)
dc.identifier.urn URN:NBN:fi:aalto-201609234493
dc.identifier.doi 10.1021/jm070501w
dc.type.version acceptedVersion


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