[en] Indoleamine 2,3-dioxygenase (rhIDO) is an enzyme mainly expressed in brain and tumor cells and catalyzing the oxidative cleavage of the indole ring of L-tryptophan through the kynurenine pathway. Furthermore this enzyme could be responsible for the eventual suppression of immune responses by blocking locally T-lymphocyte proliferation. The syntheses of 1-(2-fluoroethyl)-tryptophan (1-[19F]FETrp) and 1-((1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl)methyl)-tryptophan, two N-fluoroalkylated tryptophan derivatives, are described here. In vitro enzymatic assays with these two new potential substrates of rhIDO show that 1-[19F]FETrp is a good and specific substrate of hIDO.
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
Galleni, Moreno ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
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 :
Synthesis of N-fluoroalkyl-tryptophan and study of their biological activity as potential substrates for indoleamine 2,3-dioxygenase
Publication date :
June 2014
Event name :
French-American Chemical society Symposium - FACS XV