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Proteins in membrane mimetic systems. Insertion of myelin basic protein into microemulsion droplets.

机译:膜模拟系统中的蛋白质。将髓磷脂碱性蛋白插入微乳液液滴中。

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摘要

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.
机译:已经通过准弹性光散射研究了髓磷脂碱性蛋白插入双(2-乙基己基)磺基琥珀酸钠(AOT)的微乳液液滴中。在水与表面活性剂的低摩尔比和高摩尔比下,均根据蛋白质占有率进行测量。实验评估了填充液滴和空液滴的流体力学半径。将它们与使用蛋白质包封的水壳模型计算的值进行比较,并获得了极好的一致性。在水与表面活性剂的摩尔比低的情况下(w0 = 5.6),填充液滴的流体力学半径显着大于空液滴的半径。在这些条件下,需要大约三个空的(充满水的)液滴来构建足够大的液滴大小,以容纳单个蛋白质分子。在最大溶解度(发生在w0 = 5.6)下,发现一小部分液滴含有蛋白质聚集体。相反,在w0(22.4)的高值下的结果显示了可比较尺寸的空液滴和占据液滴的半径,并且没有聚集体。根据模型和该蛋白质与这些膜模拟系统提供的水界面的相互作用机理讨论了结果。

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