Sterol 14α-Demethylase Structure-Based Optimization of Drug Candidates for Human Infections with the Protozoan Trypanosomatidae.
Laura FriggeriTatiana Y HargroveGirish RachakondaAnna L BlobaumPaxtyn FisherGabriel Melo de OliveiraCristiane França da SilvaMaria de Nazaré C SoeiroW David NesDennis C LiottaFernando VillaltaFrederick Peter GuengerichGalina I LepeshevaPublished in: Journal of medicinal chemistry (2018)
Sterol 14α-demethylases (CYP51) are cytochrome P450 enzymes essential for sterol biosynthesis in eukaryotes and therapeutic targets for antifungal azoles. Multiple attempts to repurpose antifungals for treatment of human infections with protozoa (Trypanosomatidae) have been undertaken, yet so far none of them have revealed sufficient efficacy. VNI and its derivative VFV are two potent experimental inhibitors of Trypanosomatidae CYP51, effective in vivo against Chagas disease, visceral leishmaniasis, and sleeping sickness and currently under consideration as antiprotozoal drug candidates. However, VNI is less potent against Leishmania and drug-resistant strains of Trypanosoma cruzi and VFV, while displaying a broader spectrum of antiprotozoal activity, and is metabolically less stable. In this work we have designed, synthesized, and characterized a set of close analogues and identified two new compounds (7 and 9) that exceed VNI/VFV in their spectra of antiprotozoal activity, microsomal stability, and pharmacokinetics (tissue distribution in particular) and, like VNI/VFV, reveal no acute toxicity.
Keyphrases
- drug resistant
- endothelial cells
- multidrug resistant
- trypanosoma cruzi
- induced pluripotent stem cells
- acinetobacter baumannii
- drug induced
- single cell
- escherichia coli
- pluripotent stem cells
- liver failure
- genome wide
- oxidative stress
- emergency department
- candida albicans
- molecular docking
- cystic fibrosis
- molecular dynamics