Molecular reorganization of lipid bilayers by complement: a possible mechanism for membranolysis.
Molecular reorganization of lipid bilayers by complement: a possible mechanism for membranolysis.
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补体对脂质双层的分子重组：膜溶解的可能机制。
DOI：
10.1073/pnas.76.3.1410
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发表时间：
1979
影响因子：
11.1
通讯作者：
H. J. MULLER
中科院分区：
文献类型：
--
作者：
Alfred F. Esser;W. P. Kolb;E. Podack;H. J. MULLER
本文研究了补体的膜攻击复合物（MAC）与扁平脂质双层之间的相互作用。使用自旋标记的衍生物的磷脂和胆固醇和电子顺磁共振光谱，我们测量的MAC到双层的顺序和它的影响的双层的渗透。MAC前体组分C5 b-6、C7、C8和C9对脂膜没有任何可测量的影响。功能性C5 b-7显示出与双层表面强烈相互作用，而没有深入渗透到双层中。C5 b-8，尤其是C5 b-9的形成引起了位于烃相内的探针的光谱的各向异性的显著变化。光谱变化不是由探针旋转的变化引起的，并且在胆固醇探针的情况下，不是由于直接的探针-蛋白质相互作用。由于这些原因，我们解释的光谱变化是由磷脂MAC蛋白的强结合作用的有序双层脂质的重新取向的结果。
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.