Abstract

Candida albicans is one of the most common causes of invasive fungal infections. Azole antifungal agents are widely used as fungal antibiotics which inhibit the cytochrome P450 sterol 14 alpha-demethylase (CYP51). This study describes the homology modeling and three-dimensional model of CYP51 from C. albicans SC5314. Dope score, GA341 of Modeller, PROCHECK statistics, Ramachandran, and G-factors were used to analyze and evaluate a final model. Molecular docking identified the binding mode of the azole antifungal agents with modeled CYP51. The obtained results of Autodock program, compounds 1-4, were determined the heterocyclic nitrogen atom of azole bound to the heme iron atom in the binding site of the enzyme. Based on the results of this study, we conclude that the structural model of C. albicans SC5314 can be used in azole optimization, virtual screening and de novo inhibitor design for the discovery of new antifungal agents. This study describes the homology modeling and three-dimensional model of CYP51 from C. albicans SC5314. Dope score and GA341 of Modeller, and PROCHECK statistics, Ramachandran, and G-factors were used to analysis and evaluate of the final model.