Chongwei Bi1, Lin Wang2, Xiaodi Niu3, Hongjun Cai4, Xiaobo Zhong1, Xuming Deng2, Tiedong Wang1, Dacheng Wang5. 1. College of Animal Science, Jilin University, Changchun, 130062, China. 2. Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis/College of Veterinary Medicine, Jilin University, Changchun, China. 3. Key Laboratory of Zoonosis Research, Ministry of Education/Department of Food Quality and Safety/College of Veterinary Medicine, Jilin University, Changchun, China. 4. The College of Animal Science and Technology, Jilin Agricultural University, Changchun, China. 5. College of Animal Science, Jilin University, Changchun, 130062, China. wangdc@jlu.edu.cn.
Abstract
OBJECTIVES: To use molecular docking and dynamic simulation to investigate the inhibitory action of chlorogenic acid (CHA) and its analogues against sortase A of Staphylococcus aureus. RESULTS: Five novel, natural inhibitors with different activities were discovered for sortase A (SrtA). The inhibition mechanism of the novel inhibitors was consistent with the mechanism of CHA, which was reported previously by Wang et al. (Front Microbiol 6:1031, 2015). Based on structure-activity relationship analysis, the hydroxyl moiety (C1) of the inhibitors is critical in the catalytic region of SrtA, which could be confirmed by the calculation of the binding free energy between SrtA and the inhibitors. CONCLUSIONS: The mechanism obtained by molecular dynamics simulation is thus useful for the development of novel, selective SrtA inhibitors.
OBJECTIVES: To use molecular docking and dynamic simulation to investigate the inhibitory action of chlorogenic acid (CHA) and its analogues against sortase A of Staphylococcus aureus. RESULTS: Five novel, natural inhibitors with different activities were discovered for sortase A (SrtA). The inhibition mechanism of the novel inhibitors was consistent with the mechanism of CHA, which was reported previously by Wang et al. (Front Microbiol 6:1031, 2015). Based on structure-activity relationship analysis, the hydroxyl moiety (C1) of the inhibitors is critical in the catalytic region of SrtA, which could be confirmed by the calculation of the binding free energy between SrtA and the inhibitors. CONCLUSIONS: The mechanism obtained by molecular dynamics simulation is thus useful for the development of novel, selective SrtA inhibitors.