TY - JOUR
T1 - Melittin induces fusion of unilamellar phospholipid vesicles
AU - Morgan, Christopher G.
AU - Williamson, Heather
AU - Fuller, Stephen
AU - Hudson, Bruce
N1 - Funding Information:
This research was supported by U.S. Public Health Service Grants GM26536 and a N.I.H. Research Career Development Award (GM00476) to B.H.
PY - 1983/8/10
Y1 - 1983/8/10
N2 - 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.
AB - 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.
KW - Electron microscopy
KW - Fluorescence
KW - Melittin
KW - Membrane fusion
KW - Phospholipid vesicle
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U2 - 10.1016/0005-2736(83)90245-6
DO - 10.1016/0005-2736(83)90245-6
M3 - Article
C2 - 6871219
AN - SCOPUS:0020563750
SN - 0005-2736
VL - 732
SP - 668
EP - 674
JO - BBA - Biomembranes
JF - BBA - Biomembranes
IS - 3
ER -