[en] ABSTRACT: 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.
Disciplines :
Chemistry
Author, co-author :
Henrottin, Jean ; Université de Liège - ULiège > Centre de recherches du cyclotron
Zervosen, Astrid ; Université de Liège - ULiège > Centre de recherches du cyclotron
Lemaire, Christian ; Université de Liège - ULiège > Centre de recherches du cyclotron
Sapunaric, Frédéric
Laurent, Sophie
Van den Eynde, Benoit
Goldman, Serge
Plenevaux, Alain ; Université de Liège - ULiège > Centre de recherches du cyclotron
Luxen, André ; Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de chimie organique de synthèse
Language :
English
Title :
N1-Fluoroalkyltryptophan analogues: synthesis and in vitro study as potential substrates for indoleamine 2,3-dioxygenase
Publication date :
January 2015
Journal title :
ACS Medicinal Chemistry Letters
eISSN :
1948-5875
Publisher :
American Chemical Society, Washington, United States - District of Columbia
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