par Henrottin, Jean;Zervosen, Astrid;Lemaire, Christian;Plenevaux, Alain;Luxen, André
;Sapunaric, Frédéric;Laurent, Sophie
;Van Den Eynde, Benoit;Goldman, Serge 
Référence ACS Medicinal Chemistry Letters, 6, 3, page (260-265)
Publication Publié, 2015-03



Référence ACS Medicinal Chemistry Letters, 6, 3, page (260-265)
Publication Publié, 2015-03
Article révisé par les pairs
Résumé : | Indoleamine 2,3-dioxygenase (hIDO) is an enzyme that catalyzes the oxidative cleavage of the indole ring of l-tryptophan through the kynurenine pathway, thereby exerting immunosuppressive properties in inflammatory and tumoral tissues. The syntheses of 1-(2-fluoroethyl)-tryptophan (1-FETrp) and 1-((1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl)methyl)-tryptophan, two N1-fluoroalkylated tryptophan derivatives, are described here. In vitro enzymatic assays with these two new potential substrates of hIDO show that 1-FETrp is a good and specific substrate of hIDO. Therefore, its radioactive isotopomer, 1-[18F]FETrp, should be a molecule of choice to visualize tumoral and inflammatory tissues and/or to validate new potential inhibitors. |