title: Molecular insight into the inhibition mechanism of cyrtominetin to α-hemolysin by molecular dynamics simulation.
abstract: The protein α-hemolysin (α-HL) is a self-assembling exotoxin that binds to the membrane of a susceptible host cell. In this paper, experimental studies show that cyrtominetin (CTM) can inhibit the hemolytic activity of α-HL. To understand how CTM can affect hemolytic activity, molecular dynamics simulations were carried out for α-HL-CTM complex and these results were compared with the crystal structure of monomeric α-HL. With this approach, the analysis revealed that the inhibition of CTM involves CTM directly binding to α-HL. Due to the binding of CTM, the conformation of the critical "Loop" region was restrained. This mechanism was confirmed by the experimental data. These findings indicate that CTM hinders the lysis activity of α-HL through a novel mechanism.
authors: Department of Food Quality and Safety, Jilin University, Changchun 130062, China.
authors: Xiaodi
authors: X
authors: Niu
authors: Jiazhang
authors: J
authors: Qiu
authors: Xin
authors: X
authors: Wang
authors: Xiaohan
authors: X
authors: Gao
authors: Jing
authors: J
authors: Dong
authors: Jianfeng
authors: J
authors: Wang
authors: Hongen
authors: H
authors: Li
authors: Yu
authors: Y
authors: Zhang
authors: Xiaohan
authors: X
authors: Dai
authors: Chongjian
authors: C
authors: Lu
authors: Xuming
authors: X
authors: Deng
mesh_terms: D001427:Bacterial Toxins / Q000037:antagonists & inhibitors* / Q000737:chemistry; D044950:Flavanones / Q000737:chemistry / Q000494:pharmacology*; D006460:Hemolysin Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry; D006461:Hemolysis; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D013329:Structure-Activity Relationship
chemical_list: D001427:Bacterial Toxins; D044950:Flavanones; D006460:Hemolysin Proteins; C583780:cyrtominetin; C021091:staphylococcal alpha-toxin