1415903-52-4Relevant academic research and scientific papers
Synthesis and evaluation of substrate analogue inhibitors of trypanothione reductase
Duyzend, Michael H.,Clark, Christopher T.,Simmons, Shayna L.,Johnson, Wade B.,Larson, Anna M.,Leconte, Aaron M.,Wills, Andrew W.,Ginder-Vogel, Matthew,Wilhelm, April K.,Czechowicz, Josephine A.,Alberg, David G.
, p. 784 - 794 (2013/02/23)
Trypanothione reductase (TR) is found in the trypanosomatid parasites, where it catalyses the NADPH-dependent reduction of the glutathione analogue, trypanothione, and is a key player in the parasite's defenses against oxidative stress. TR is a promising target for the development of antitrypanosomal drugs; here, we report our synthesis and evaluation of compounds 3-5 as low micromolar Trypanosoma cruzi TR inhibitors. Although 4 and 5 were designed as potential irreversible inhibitors, these compounds, as well as 3, displayed reversible competitive inhibition. Compound 3 proved to be the most potent inhibitor, with a Ki=2 μM.
