Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide-containing liposomes as a model for outer membranes of gram-negative bacteria.
FEBS Lett
; 449(2-3): 221-4, 1999 Apr 23.
Article
em En
| MEDLINE
| ID: mdl-10338136
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Fosfatidilcolinas
/
Proteínas da Membrana Bacteriana Externa
/
Lipopolissacarídeos
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Peptídeos Catiônicos Antimicrobianos
/
Proteínas de Xenopus
/
Bactérias Gram-Negativas
/
Antibacterianos
Idioma:
En
Ano de publicação:
1999
Tipo de documento:
Article