Abstract
The sesquiterpene lactone 4,15-isoatriplicolide tiglate 1 was recently discovered as an extremely potent trypanocidal agent with an in vitro IC50 of only 15 nM against Trypanosoma brucei rhodesiense, causative pathogen of East African Human Trypanosomiasis (HAT) [1]. Trypanosomatids possess a unique mechanism to maintain their redox state and defend themselves against oxidative stress, in which the glutathione/glutathione reductase system, serving this purpose in other Eukaryotes, is replaced by Trypanothione/Trypanothione reductase (TR). TR is therefore a potential target for new leads and drugs against HAT and related diseases [2]. In an attempt to identify potential molecular targets of the isoatriplicolide ester in trypanosomes, we have investigated the possibility that it inhibits the parasites' most crucial redox enzyme.
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