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(S)-1-(Pent-4'-enoyl)-4-(hydroxymethyl)-azetidin-2-one derivatives as inhibitors of human fatty acid amide hydrolase (hFAAH): synthesis, biological evaluation and molecular modelling.
Caruano, Joséphine; Feledziak, Marion; Labar, Geoffray; Michaux, Catherine; Perpète, Eric A; Muccioli, Giulio G; Robiette, Raphaël; Marchand-Brynaert, Jacqueline.
Afiliación
  • Caruano J; Institut de la Matière Condensée et des Nanosciences (IMCN), Université catholique de Louvain (UCL) , Louvain-la-Neuve , Belgium .
J Enzyme Inhib Med Chem ; 29(5): 654-62, 2014 Oct.
Article en En | MEDLINE | ID: mdl-24102523
A series of lipophilic ester derivatives (2a-g) of (S)-1-(pent-4'-enoyl)-4-(hydroxymethyl)-azetidin-2-one has been synthesised in three steps from (S)-4-(benzyloxycarbonyl)-azetidin-2-one and evaluated as novel, reversible, ß-lactamic inhibitors of endocannabinoid-degrading enzymes (human fatty acid amide hydrolase (hFAAH) and monoacylglycerol lipase (hMAGL)). The compounds showed IC50 values in the micromolar range and selectivity for hFAAH versus hMAGL. The unexpected 1000-fold decrease in activity of 2a comparatively to the known regioisomeric structure 1a (i.e. lipophilic chains placed on N1 and C3 positions of the ß-lactam core) could be explained on the basis of docking studies into a revisited model of hFAAH active site, considering one or two water molecules in interaction with the catalytic triad.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Azetidinas / Modelos Moleculares / Inhibidores Enzimáticos / Amidohidrolasas Límite: Humans Idioma: En Revista: J Enzyme Inhib Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2014 Tipo del documento: Article País de afiliación: Bélgica Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Azetidinas / Modelos Moleculares / Inhibidores Enzimáticos / Amidohidrolasas Límite: Humans Idioma: En Revista: J Enzyme Inhib Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2014 Tipo del documento: Article País de afiliación: Bélgica Pais de publicación: Reino Unido