Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1373742 | Bioorganic & Medicinal Chemistry Letters | 2009 | 5 Pages |
Abstract
Novel quinazoline-type compounds were designed as inhibitors of the parasite specific enzyme trypanothione reductase (TR), and their biological activities were evaluated. Some of our compounds inhibited TR, showed selectivity for TR over human glutathione reductase, and inhibited parasite growth in vitro. We propose that the quinazoline framework is a privileged structure that can be purposely modified to design novel TR inhibitors. Furthermore, the use of privileged motifs might emerge as an innovative approach to antiparasitic lead candidates.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Andrea Cavalli, Federica Lizzi, Salvatore Bongarzone, Reto Brun, R. Luise Krauth-Siegel, Maria Laura Bolognesi,