16547-59-4Relevant academic research and scientific papers
N 1-fluoroalkyltryptophan analogues: Synthesis and in vitro study as potential substrates for indoleamine 2,3-dioxygenase
Henrottin, Jean,Zervosen, Astrid,Lemaire, Christian,Sapunaric, Frédéric,Laurent, Sophie,Van Den Eynde, Benoit,Goldman, Serge,Plenevaux, Alain,Luxen, André
supporting information, p. 260 - 265 (2015/03/30)
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.
