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Biophysical Journal 73: 831-838 (1997)
© 1997 the Biophysical Society

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Pore formation and translocation of melittin.

K Matsuzaki, S Yoneyama and K Miyajima

Faculty of Pharmaceutical Sciences, Kyoto University, Japan. katsumim@pharm.kyoto-u.ac.jp

ABSTRACT

Melittin, a bee venom, is a basic amphiphilic peptide, which mainly acts on the lipid matrix of membranes, lysing various cells. To elucidate the molecular mechanism, we investigated its interactions with phospholipid vesicles. The peptide formed a pore with a short lifetime in the membrane, as revealed by the release of an anionic fluorescent dye, calcein, from the liposomes. Our new double-labeling method clarified that the pore size increased with the peptide-to-lipid ratio. Upon the disintegration of the pore, a fraction of the peptides translocated across the bilayer. The pore formation was coupled with the translocation, which was proved by three fluorescence experiments recently developed by our laboratory. A novel model for the melittin pore formation was discussed in comparison with other pore-forming peptides.




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