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The synthesis and inhibitory activity of dethiotrypanothione and analogues against trypanothione reductase.


ABSTRACT: Trypanothione reductase (TR) catalyzes the NADPH-dependent reduction of trypanothione disulfide (1). TR plays a central role in the trypanosomatid parasite's defense against oxidative stress and has emerged as a promising target for antitrypanosomal drugs. We describe the synthesis and activity of dethiotrypanothione and analogues (2-4) as inhibitors of Trypanosoma cruzi TR. The syntheses of these macrocycles feature ring-closing olefin metathesis (RCM) reactions catalyzed by ruthenium catalyst 17. Derivative 4 is our most potent inhibitor with a Ki=16 microM.

SUBMITTER: Czechowicz JA 

PROVIDER: S-EPMC2528058 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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The synthesis and inhibitory activity of dethiotrypanothione and analogues against trypanothione reductase.

Czechowicz Josephine A JA   Wilhelm April K AK   Spalding Maroya D MD   Larson Anna M AM   Engel Linnea K LK   Alberg David G DG  

The Journal of organic chemistry 20070417 10


Trypanothione reductase (TR) catalyzes the NADPH-dependent reduction of trypanothione disulfide (1). TR plays a central role in the trypanosomatid parasite's defense against oxidative stress and has emerged as a promising target for antitrypanosomal drugs. We describe the synthesis and activity of dethiotrypanothione and analogues (2-4) as inhibitors of Trypanosoma cruzi TR. The syntheses of these macrocycles feature ring-closing olefin metathesis (RCM) reactions catalyzed by ruthenium catalyst  ...[more]

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