Andrews A L, Atkinson D, Barratt M D, Finer E G, Hauser H, Henry R, Leslie R B, Owens N L, Phillips M C, Robertson R N
Eur J Biochem. 1976 May 1;64(2):549-63. doi: 10.1111/j.1432-1033.1976.tb10335.x.
The detailed molecular structure of the complex formed by the apoprotein from porcine high density lipoprotein and dimyristoly phosphatidylcholine (lecithin) has been investigated by a range of physical techniques. The complex, an oblate ellipsoid with major axis 11.0 nm and minor axis 5.5 nm (see the accompanying paper), is comprised of a section of lecithin bilayer with apoprotein at the surface. The main site of interaction between protein and lipid is in the lipid glycerophosphorylcholine group region; as with native high density lipoprotein the surface of the particle consists of a mosaic of lecithin polar groups and protein. The formation of this mosaic reduces the cooperativity of the lecithin chain motions and changes the curvature of the lipid-water interface, as compared to a bilayer. Otherwise, there are no major changes in lecithin motions indicating that no strong binding of lipid to protein occurs. The interaction involves the intercalation of amphipathic, 60% alpha-helical, apoprotein molecules among the lecithin molecules so that the protein residues at the lipid-water interface. The apoprotein has a high affinity for the lipid-water interface but specific lipid-protein interactions are not involved.
通过一系列物理技术研究了猪高密度脂蛋白脱辅基蛋白与二肉豆蔻酰磷脂酰胆碱（卵磷脂）形成的复合物的详细分子结构。该复合物是一个扁长椭球体，长轴为11.0纳米，短轴为5.5纳米（见随附论文），由一段卵磷脂双层和表面的脱辅基蛋白组成。蛋白质与脂质之间的主要相互作用位点位于脂质甘油磷酸胆碱基团区域；与天然高密度脂蛋白一样，颗粒表面由卵磷脂极性基团和蛋白质组成的镶嵌物构成。与双层相比，这种镶嵌物的形成降低了卵磷脂链运动的协同性，并改变了脂质 - 水界面的曲率。否则，卵磷脂运动没有重大变化，这表明脂质与蛋白质之间没有强烈结合。这种相互作用涉及两亲性的、60%为α - 螺旋的脱辅基蛋白分子插入卵磷脂分子之间，使得蛋白质残基位于脂质 - 水界面。脱辅基蛋白对脂质 - 水界面具有高亲和力，但不涉及特定的脂质 - 蛋白质相互作用。
