Chatenay D, Urbach W, Cazabat A M, Vacher M, Waks M
Biophys J. 1985 Dec;48(6):893-8. doi: 10.1016/S0006-3495(85)83851-0.
The insertion of myelin basic protein into microemulsion droplets of sodium bis (2-ethylhexyl) sulfosuccinate (AOT) has been studied by quasi-elastic light scattering. Measurements were made at both low and high molar ratios of water to surfactant, as a function of protein occupancy. The hydrodynamic radii of filled and empty droplets were experimentally evaluated. These were compared to values calculated using a water shell model of protein encapsulation, and excellent agreement was obtained. At low molar ratio of water to surfactant (w0 = 5.6), the hydrodynamic radius of filled droplets is significantly larger than the radius of empty ones. Under these conditions, about three empty (water-filled) droplets are required to build up a droplet of sufficient size to accommodate a single protein molecule. At maximum solubilization, which occurs at w0 = 5.6, a small fraction of droplets are found containing protein aggregates. In contrast, results at high values of w0 (22.4) reveal radii for empty and occupied droplets of comparable dimension, and the absence of aggregates. The results are discussed in terms of the model and the mechanism of interaction of this protein with the aqueous interfaces provided by these membrane-mimetic systems.
通过准弹性光散射研究了髓鞘碱性蛋白插入双（2-乙基己基）磺基琥珀酸钠（AOT）微乳液滴中的情况。在水与表面活性剂的低摩尔比和高摩尔比条件下，均根据蛋白质占有率进行了测量。通过实验评估了填充和未填充液滴的流体动力学半径。并将这些结果与使用蛋白质包封水壳模型计算的值进行了比较，结果吻合良好。在水与表面活性剂的低摩尔比（w0 = 5.6）下，填充液滴的流体动力学半径明显大于未填充液滴的半径。在这些条件下，大约需要三个未填充（充满水）的液滴才能形成一个足够大的液滴来容纳单个蛋白质分子。在w0 = 5.6时达到最大增溶，发现一小部分液滴含有蛋白质聚集体。相比之下，w0值较高（22.4）时的结果显示，未填充和填充液滴的半径尺寸相当，且不存在聚集体。根据该模型以及这种蛋白质与这些模拟膜系统提供的水相界面相互作用的机制对结果进行了讨论。
