Pore formation and translocation of melittin.
AUTOR(ES)
Matsuzaki, K
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1180979Documentos Relacionados
- Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin.
- NMR studies of a complex of deuterated calmodulin with melittin.
- Inhibition of a plant virus infection by analogs of melittin.
- Osmotic and pH transmembrane gradients control the lytic power of melittin.
- Viral DNA synthesized in vitro by avian retrovirus particles permeabilized with melittin. I. Kinetics of synthesis and size of minus- and plus-strand transcripts.