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Leishmania amazonensis trypanothione reductase: Evaluation of the effect of glutathione analogs on parasite growth, infectivity and enzyme activity

2007; Taylor & Francis; Volume: 22; Issue: 1 Linguagem: Inglês

10.1080/14756360600920180

1475-6374

Denise Barçante Castro‐Pinto, Edson L. S. Lima, Andréa Sousa da Cunha, Marcelo Genestra, Rosa Maria De Léo, Fabiane Pereira Monteiro, Leonor L. Leon,

Insect Pest Control Strategies

Trypanothione reductase (TR) is a major enzyme in trypanosomatids. Its substrate, trypanothione is a molecule containing a tripeptide (L-glutamic acid-cysteine-glycine) coupled to a polyamine, spermidine. This redox system (TR/Trypanothione) is vital for parasite survival within the host cell and has been described as a good target for chemotherapy anti-Leishmania. The use of tripeptides analogs of glutathione would result in a decrease in trypanothione synthesis and as a consequence in TR activity. In this work, besides the enzyme potential inhibition, it also evaluated the influence of those analogs on parasite growth and on its infective capacity. The results showed a significant effect on parasite growth and infectivity and in addition TR activity was highly inhibited. These results are very promising, suggesting a potential use of those analogs as therapeutic drugs against experimental diseases caused by trypanosomatids.