Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase.

@article{Ponasik1995KukoamineAA,
  title={Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase.},
  author={James A Ponasik and Corey Strickland and Carlos Faerman and Savvas N. Savvides and P. Andrew Karplus and B. Ganem},
  journal={The Biochemical journal},
  year={1995},
  volume={311 ( Pt 2)},
  pages={371-5}
}
The enzyme trypanothione reductase (TR), together with its substrate, the glutathione-spermidine conjugate trypanothione, plays an essential role in protecting parasitic trypanosomatids against oxidative stress and is a target for drug design. Here we show that a naturally occurring spermine derivative, the antihypertensive agent kukoamine A [N1N12-bis(dihydrocaffeoyl)-spermine] inhibits TR as a mixed inhibitor (Ki = 1.8 microM, Kii = 13 microM). Kukoamine shows no significant inhibition of… CONTINUE READING