Design, synthesis, and antifungal activities of novel 1H-triazole derivatives based on the structure of the active site of fungal lanosterol 14 alpha-demethylase (CYP51)

Chem Biodivers. 2007 Jul;4(7):1472-9. doi: 10.1002/cbdv.200790125.

Abstract

A series of fluconazole (1) analogues, compounds 3a-k, were prepared as potential antifungal agents. They were designed by computational docking experiments to the active site of the cytochrome P450 14alpha-sterol demethylase (CYP51), whose crystal structure is known. Preliminary biological tests showed that most of the target compounds exhibit significant activities against the eight most-common pathogenic fungi. Thereby, the most potent congener, 1-[(4-tert-butylbenzyl)(cyclopropyl)amino]-2-(2,4-difluorophenyl)-3-(1H-1,2,4-triazol-1-yl)propan-2-ol (3j), was found to exhibit a broad antifungal spectrum, being more active against Candida albicans, Candida tropicalis, Cryptococcus neoformans, Microsporum canis, and Trichophyton rubrum (MIC80 < 0.125 microg/ml) than the standard clinical drug itraconazole (2). The observed affinities of the lead molecules towards CYP51 indicate that a cyclopropyl residue enhances binding to the target enzyme. Our results may provide some guidance for the development of novel triazole-based antifungal lead structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antifungal Agents / chemical synthesis*
  • Antifungal Agents / pharmacology
  • Binding Sites / drug effects
  • Binding Sites / physiology
  • Chemistry, Pharmaceutical / methods
  • Cytochrome P-450 Enzyme System / chemical synthesis*
  • Cytochrome P-450 Enzyme System / metabolism
  • Drug Design*
  • Hydrogen
  • Microbial Sensitivity Tests / methods
  • Oxidoreductases / chemical synthesis*
  • Oxidoreductases / metabolism
  • Sterol 14-Demethylase
  • Triazoles / chemical synthesis*
  • Triazoles / pharmacology

Substances

  • Antifungal Agents
  • Triazoles
  • Hydrogen
  • Cytochrome P-450 Enzyme System
  • Oxidoreductases
  • Sterol 14-Demethylase