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Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide‐containing liposomes as a model for outer membranes of Gram‐negative bacteria
Author(s) -
Matsuzaki Katsumi,
Sugishita Ken-ichi,
Miyajima Koichiro
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00443-3
Subject(s) - magainin , peptide , lipopolysaccharide , liposome , antimicrobial peptides , chemistry , membrane , phosphatidylcholine , vesicle , bacterial outer membrane , lipid a , biophysics , gram negative bacteria , lipid bilayer , lipopeptide , biochemistry , bacteria , phospholipid , biology , escherichia coli , gene , endocrinology , genetics
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 Mg 2+ , 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.