Homology modeling, molecular docking and spectra assay studies of sterol 14[alpha]-demethylase from Penicillium digitatum

• Published in: Biotechnology letters Vol. 33; no. 10; p. 2005
• Main Authors: Li, Shuxiang, Zhang, Jianhua, Cao, Shufen, Han, Rui, Yuan, Yongze, Yang, Jiangke, Yan, Yunjun, Liu, Deli
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Nature B.V 01.10.2011
• Subjects: Binding sites; Fungicides; Molecular biology; Plant diseases; Spectrum analysis
• ISSN: 0141-5492; 1573-6776
• DOI: 10.1007/s10529-011-0657-x

Sterol 14α-demethylase from Penicillium digitatum (PdCYP51) is a prime target of antifungal drugs for citrus disease in plants. To design novel antifungal compounds, a homology model of PdCYP51 was constructed using the recently reported crystal structure of human CYP51 as the template. Molecular docking was performed to investigate the interaction of four commercial fungicides with the modeled enzyme. The side chain of these compounds interplayed with PdCYP51 mainly through hydrophobic and van der Waals interactions. Biochemical spectra analysis of inhibitors combined with PdCYP51 are also compatible with the docking results. This is the first molecular modeling for PdCYP51 based on the eukaryotic crystal structure of CYP51. The structural information and binding site mapping of PdCYP51 for different inhibitors obtained from this study could aid in screening and designing new antifungal compounds targeting this enzyme.[PUBLICATION ABSTRACT]