Melittin induces fusion of unilamellar phospholipid vesicles

Christopher G. Morgan, Heather Williamson, Stephen Fuller, Bruce Hudson

Research output: Contribution to journalArticlepeer-review

66 Scopus citations


Melittin, the soluble lipophilic peptide of bee venom, causes fusion of phospholipid vesicles when vesicle suspensions are heated or cooled through their thermal phase transition. Fusion was detected using a new photochemical method (Morgan, C.G., Hudson, B. and Wolber, P. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 26-30) which monitors lipid mixing. Electron microscopy and gel filtration confirmed that most of the lipid formed large vesicular structures. Fluorescence experiments with a water-soluble, membrane-impermeable complex of terbium (Wilschut, J. and Papahadjopoulos, D. (1979) Nature 281, 690-692) demonstrate that these ionic contents are released during fusion. The large structures formed by melittin-induced fusion are impermeable to these ions and are resistant to further fusion. This is in contrast to the behavior observed for the cationic detergent cetyltrimethylammonium bromide (CETAB). The large size of the vesicles formed, the extreme speed of the fusion event and the appearance of electron microscope images of the vesicles prior to fusion suggest that the mechanism of the fusion process includes a preaggregation step.

Original languageEnglish (US)
Pages (from-to)668-674
Number of pages7
JournalBBA - Biomembranes
Issue number3
StatePublished - Aug 10 1983
Externally publishedYes


  • Electron microscopy
  • Fluorescence
  • Melittin
  • Membrane fusion
  • Phospholipid vesicle

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


Dive into the research topics of 'Melittin induces fusion of unilamellar phospholipid vesicles'. Together they form a unique fingerprint.

Cite this