Molecular reorganization of lipid bilayers by complement: a possible mechanism for membranolysis.
The interaction between the membrane attack complex (MAC) of complement and flat lipid bilayers was investigated. Using spin-labeled derivatives of phospholipids and cholesterol and electron paramagnetic resonance spectroscopy, we measured the penetration of the MAC into bilayers and its influence on the order of bilayers. The MAC precursor components C5b--6, C7, C8, and C9 did not exert any measurable influence on lipid membranes. Functional C5b--7 was shown to interact strongly with the bilayer surface without deep penetration into the bilayer. Formation of C5b--8 and especially C5b--9 caused a marked change in the anisotropy of spectra from probes located within the hydrocarbon phase. The spectral changes are not caused by changes in probe rotation and, in the case of the cholesterol probes, are not due to direct probe--protein interactions. For these reasons we interpret the spectral changes to be the result of reorientation of ordered bilayer lipids effected by strong binding of phospholipids to MAC proteins.
D002784:Cholesterol; D003165:Complement System Proteins; D004578:Electron Spin Resonance Spectroscopy; D008567:Membranes, Artificial; D008954:Models, Biological; D008968:Molecular Conformation; D010713:Phosphatidylcholines; D011485:Protein Binding; D011487:Protein Conformation; D013113:Spin Labels
D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D013113:Spin Labels; D003165:Complement System Proteins; D002784:Cholesterol