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Chemical validation of trypanothione synthetase: a potential drug target for human trypanosomiasis.

Authors :
Torrie LS
Wyllie S
Spinks D
Oza SL
Thompson S
Harrison JR
Gilbert IH
Wyatt PG
Fairlamb AH
Frearson JA
Source :
The Journal of biological chemistry [J Biol Chem] 2009 Dec 25; Vol. 284 (52), pp. 36137-36145. Date of Electronic Publication: 2009 Oct 14.
Publication Year :
2009

Abstract

In the search for new therapeutics for the treatment of human African trypanosomiasis, many potential drug targets in Trypanosoma brucei have been validated by genetic means, but very few have been chemically validated. Trypanothione synthetase (TryS; EC 6.3.1.9; spermidine/glutathionylspermidine:glutathione ligase (ADP-forming)) is one such target. To identify novel inhibitors of T. brucei TryS, we developed an in vitro enzyme assay, which was amenable to high throughput screening. The subsequent screen of a diverse compound library resulted in the identification of three novel series of TryS inhibitors. Further chemical exploration resulted in leads with nanomolar potency, which displayed mixed, uncompetitive, and allosteric-type inhibition with respect to spermidine, ATP, and glutathione, respectively. Representatives of all three series inhibited growth of bloodstream T. brucei in vitro. Exposure to one of our lead compounds (DDD86243; 2 x EC(50) for 72 h) decreased intracellular trypanothione levels to <10% of wild type. In addition, there was a corresponding 5-fold increase in the precursor metabolite, glutathione, providing strong evidence that DDD86243 was acting on target to inhibit TryS. This was confirmed with wild-type, TryS single knock-out, and TryS-overexpressing cell lines showing expected changes in potency to DDD86243. Taken together, these data provide initial chemical validation of TryS as a drug target in T. brucei.

Details

Language :
English
ISSN :
1083-351X
Volume :
284
Issue :
52
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
19828449
Full Text :
https://doi.org/10.1074/jbc.M109.045336