Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide‐containing liposomes as a model for outer membranes of Gram‐negative bacteria

FEBS Letters

Sugishita, Ken-ichi¹  Matsuzaki, Katsumi¹  Miyajima, Koichiro¹ 

[1] Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan

关键词: Magainin;    Lipopolysaccharide;    Lipid A;    Outer membrane;    Membrane permeabilization;   

DOI  :  10.1016/S0014-5793(99)00443-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

F12W-magainin 2 preferentially interacted with lipopolysaccharide-containing bilayers, permeabilizing the membranes, compared with lipopolysaccharide-free phosphatidylcholine vesicles. Using this system, we demonstrated for the first time that the magainin peptide forms a helix upon binding to lipopolysaccharide. Incorporation of lipid A into phosphatidylcholine liposomes also enhanced interactions with the peptide. The presence of Mg²⁺, which nullifies the peptide's antibacterial activity against Gram-negative bacteria, again weakened the interactions between the peptide and lipopolysaccharide-doped bilayers. This system seems to be useful for investigating the molecular details of peptide-lipopolysaccharide interactions.

【 授权许可】

Unknown