Esser A F, Kolb W P, Podack E R, Müller-Eberhard H J
Proc Natl Acad Sci U S A. 1979 Mar;76(3):1410-4. doi: 10.1073/pnas.76.3.1410.
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.
研究了补体膜攻击复合物(MAC)与扁平脂质双层之间的相互作用。我们使用磷脂和胆固醇的自旋标记衍生物以及电子顺磁共振光谱,测量了MAC对双层的渗透及其对双层有序性的影响。MAC前体成分C5b-6、C7、C8和C9对脂质膜没有任何可测量的影响。功能性C5b-7被证明与双层表面强烈相互作用,但不会深入双层内部。C5b-8尤其是C5b-9的形成导致位于烃相内的探针光谱各向异性发生显著变化。光谱变化不是由探针旋转的变化引起的,对于胆固醇探针而言,也不是由于直接的探针-蛋白质相互作用。基于这些原因,我们将光谱变化解释为磷脂与MAC蛋白的强结合导致有序双层脂质重新定向的结果。