Biochemistry 1995 Oct 03;3439:12553-9.

Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers.

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The kinetics of the pore formation by magainin 2, an antimicrobial peptide from Xenopus laevis, in lipid vesicles was investigated. The pore formation was estimated by the efflux of a fluorescent dye, calcein, from large unilamellar vesicles composed of egg yolk phosphatidylglycerol. The time courses of the dye release were well-described by a novel model in which the peptide molecules translocate from the outer to the inner monolayer by forming a pore. The concentration dependence of the leakage rate suggested that the pore consists of pentameric magainin. The obtained kinetic parameters estimate that, at a lipid-to-peptide molar ratio of 117, 9 pores with a lifetime of 40 microseconds open per second per vesicle in the initial phase. The apparent deactivation of the pore with increasing time can be ascribed to the reduced peptide density in the outer leaflet due to the translocation. Incorporation of phosphatidylcholine destabilized the pore, indicating the importance of anionic lipids in the stable pore formation.

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Species referenced: Xenopus laevis
Genes referenced: magainins