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. 1997 Aug;73(2):831–838. doi: 10.1016/S0006-3495(97)78115-3

Pore formation and translocation of melittin.

K Matsuzaki 1, S Yoneyama 1, K Miyajima 1
PMCID: PMC1180979  PMID: 9251799

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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Selected References

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