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PAGE \* MERGEFORMAT 17
Antimicrobial peptide homologues Thanatin Study on the mechanism
Of: Wu Hongbin, Ding Jiaxuan, Zhao Rui, Fan Xiaobo, Ma Yihua, Shenzi Long, Xi Tao, Wu ball
[Abstract] Objective: To study the antimicrobial peptide Thanatin homologues (S thanatin, Ts), and mechanism of action targets. METHODS: Ts with lipopolysaccharide (LPS) of the binding experiments, with different components of the calcium phospholipid prepared package yellow pigment and the liposome membrane to simulate the role of peptides, other peptides can promote cell of -galactosidase in the release to indicate changes in membrane permeability, using electron microscopy the role of bacteria in the subject after antimicrobial peptides ultrastructural changes. Results: Ts with a strong affinity with LPS (50% effect concentration of 50 g ml-1), peptides on liposomes have a strong disruptive effect, the presence of cholesterol inhibited to some extent this role. electron microscope image shows no effect of cell membrane dosing relatively clear smooth edges, and the role of the cell membrane by peptides is very irregular, and there are broken and the contents of the release. Conclusions: clarify the role of peptides by Ts disrupt the cell membrane phospholipids play in the bactericidal effect, and most likely through electrostatic interactions with the LPS binding.
[Keywords:] peptide; S thanatin; phospholipids; membrane; mechanism
[Abstract] Objective: To investigate the antibacterial mechanism of thanatin analog, antimicrobial peptide S thanatin (Ts). Methods: In this study, we investigated its lipopolysaccharide (LPS) binding and neutralizing activity in vitro. We also investigated the effect of the presence of cholesterol on the interactions of the antimicrobial peptide Ts with phosphatidylcholine (PC) model membrane systems. Diffusion of extracellular o nitrophenyl D galactopyranoside (ONPG) into the cytoplasm of E. coli cells was monitored by measuring the product
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