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Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs.

Abstract : Leishmaniasis is a neglected disease that kills 60,000 people worldwide, and which is caused by the protozoa Leishmania. The enzymes of the trypanothione pathway: trypanothione synthetase-amidase, trypanothione reductase (TR) and tryparedoxin-dependent peroxidase are absent in human hosts, and are essential for parasite survival and druggable. The most promising target is trypanothione synthetase-amidase, which has been also chemically validated. However, the structural data presented in this review show that TR also should be considered as a good target. Indeed, it is strongly inhibited by silver- and gold-containing compounds, which are active against Leishmania parasites and can be used for the development of novel antileishmanial agents. Moreover, TR trypanothione-binding site is not featureless but contains a sub-pocket where inhibitors bind, potentially useful for the design of new lead compounds.
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https://hal-riip.archives-ouvertes.fr/pasteur-01023953
Contributor : Istituto Pasteur Fondazione Cenci Bolognetti <>
Submitted on : Tuesday, July 15, 2014 - 2:54:21 PM
Last modification on : Tuesday, April 30, 2019 - 2:46:04 PM

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Gianni Colotti, Paola Baiocco, Annarita Fiorillo, Alberto Boffi, Elena Poser, et al.. Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs.. Future Medicinal Chemistry, Future Science, 2013, 5 (15), pp.1861-75. ⟨10.4155/fmc.13.146⟩. ⟨pasteur-01023953⟩

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