Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines.
The binding of melittin to phosphatidylethanolamine model systems and its influence on the supramolecular organization of the lipid were investigated with binding assays, differential scanning calorimetry, 31P NMR, freeze-fracture electron microscopy, and small-angle X-ray scattering. The results are compared with binding to an analogous phosphatidylcholine and structural consequences thereof. Melittin binds with similar affinity to both lipid types in the liquid-crystalline state; at gel-phase temperatures, in contrast, interaction with phosphatidylethanolamine is much weaker and does not lead to the bilayer fragmentation observed for phosphatidylcholines. With regard to phosphatidylethanolamine polymorphism, it is shown that melittin acts as an inhibitor of HII-phase formation and as a stabilizer of the bilayer organization. It is demonstrated that the remarkable variety of effects of melittin on the polymorphism of different membrane phospholipids can be understood in a relatively simple concept, taking into account the relative position and the shape of the interacting components.
Batenburg
A M
AM
Department of Biochemistry, State University of Utrecht, The Netherlands.
van Esch
J H
JH
de Kruijff
B
B
D001514:Bee Venoms; D002152:Calorimetry, Differential Scanning; D005614:Freeze Fracturing; D009682:Magnetic Resonance Spectroscopy; D008555:Melitten; D008854:Microscopy, Electron; D008954:Models, Biological; D008968:Molecular Conformation; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014961:X-Ray Diffraction
D001514:Bee Venoms; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D008555:Melitten