AI Article Synopsis
- Indoleamine 2,3-dioxygenase (hIDO) is an enzyme that contributes to immunosuppression by breaking down l-tryptophan in inflammatory and tumor environments.
- The study describes the creation of two new compounds, 1-(2-fluoroethyl)-tryptophan (1-FETrp) and a related derivative, which serve as potential substrates for hIDO.
- In tests, 1-FETrp was identified as a suitable and specific substrate for hIDO, suggesting it could be used alongside its radioactive version, 1-[(18)F]FETrp, for imaging tumors and inflammation or assessing new treatments.
Article 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 N (1)-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-[(18)F]FETrp, should be a molecule of choice to visualize tumoral and inflammatory tissues and/or to validate new potential inhibitors.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4360160 | PMC |
| http://dx.doi.org/10.1021/ml500385d | DOI Listing |
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