Modulation by glycosphingolipids of membrane-membrane interactions induced by myelin basic protein and melittin.
Modulation by glycosphingolipids of membrane-membrane interactions induced by myelin basic protein and melittin.
复制标题
鞘糖脂对髓磷脂碱性蛋白和蜂毒肽诱导的膜-膜相互作用的调节。
DOI：
10.1016/0005-2736(92)90260-s
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Yu,RK
中科院分区：
文献类型：
--
作者：
Maggio,B;Yu,RK
采用单层小泡模型，比较研究了不同长度和电荷的鞘糖脂（GSL）对髓鞘碱性蛋白（MBP）和蜂毒肽（Mel）诱导的膜-膜相互作用的影响。MBP诱导囊泡快速聚集和紧密的膜附着。与膜沉积相比，MBP诱导的脂质双层的合并和囊泡融合是较慢且不太广泛的过程。伴随这些现象的膜通透性的变化是小的。MBP的色氨酸区域在与囊泡相互作用时保持在相当极性的环境中;其对NO3或丙烯酰胺淬灭的可及性取决于膜中GSL的类型。Mel的Trp区域更深地插入到脂质双层中，并且其对水性猝灭剂的可及性较少依赖于GSL的寡糖链的变化。与MBP相比，Mel诱导更快和更广泛的膜并置和双层合并。在Mel存在下发生广泛的囊泡破坏。带负电荷的GSL促进膜接近和囊泡聚集，但中性或酸性GSL的寡糖链长度的增加降低了由任一蛋白诱导的囊泡之间的相互作用。这种效应与MBP和Mel插入膜的不同方式无关。我们的研究结果表明，调制的寡糖链上的蛋白质诱导的相互作用之间的双层含有GSL的可能超出了当地的基础蛋白质和脂质之间的分子相互作用的水平。
The effect of glycosphingolipids (GSLs) with oligosaccharide chains of different length and charge on membrane-membrane interactions induced by myelin basic protein (MBP) or melittin (Mel) was comparatively investigated with small unilamellar vesicles. MBP induces a fast vesicle aggregation and close membrane apposition. Merging of lipid bilayers and vesicle fusion induced by MBP are slower and less extensive processes compared to membrane apposition. The changes of membrane permeability concomitant to these phenomena are small. The Trp region of MBP remains in a rather polar environment when interacting with vesicles; its accessibility to NO3or acrylamide quenching depends on the type of GSLs in the membrane. The Trp region of Mel is inserted more deeply into the lipid bilayer and its accessibility to the aqueous quenchers is less dependent on variations of the oligosaccharide chain of the GSLs. Mel induces a faster and more extensive membrane apposition and bilayer merging than does MBP. Extensive vesicle disruption occurs in the presence of Mel. Negatively charged GSLs facilitate membrane proximity and vesicle aggregation but an increase of the oligosaccharide chain length of either neutral or acidic GSLs decreases the interaction among vesicles that are induced by either protein. This effect is independent of the different mode of insertion of MBP and Mel into the membrane. Our results suggest that the modulation by the oligosaccharide chain on the protein-induced interactions between bilayers containing GSLs is probably exerted beyond the level of local molecular interactions between the basic proteins and the lipids.