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arXiv 0709.3536cond-mat.softcond-mat.dis-nn
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蛋白质的动力学:接目镜匀浆的稀和浓胶体悬浮液的光散射研究

Dynamics of proteins: Light scattering study of dilute and dense colloidal suspensions of eye lens homogenates

A. Giannopoulou, A. J. Aletras, N. Pharmakakis, G. N. Papatheodorou, S. N. Yannopoulos

摘要:

我们报告了一个动态光散射研究的牛晶状体匀浆蛋白悬浮液在条件(pH值和离子强度)类似的生理。在20 ℃和37 ℃两种温度下,在从非常稀的极限到接近生理晶状体浓度的密集状态的广泛浓度范围内收集光散射数据。与实验数据的比较,从完整的牛晶状体先进的分散体和透镜在相似的浓度之间的差异。在稀释制度中,两个散射实体被检测到,并确定与长期,自扩散模式的α-晶体蛋白及其聚集体,这自然存在于晶状体核。自扩散系数对温度不敏感,而集体扩散系数强烈依赖于温度,揭示了随着温度的降低,净排斥粒子间力的减少。虽然没有严格的理论方法对颗粒扩散性能的多组分,非理想的硬球,多分散系统,作为这里研究的悬浮液,在现有的理论方法的上下文中的长时间,自扩散系数的体积分数的依赖性进行了讨论。这项研究旨在提供一些了解完整晶状体的复杂光散射模式和负责晶状体透明度的组成蛋白质之间的相互作用。这将导致理解在病理条件下导致晶状体混浊(白内障)的特定蛋白质相互作用的基本机制。

英文摘要:

We report a dynamic light scattering study on protein suspensions of bovine lens homogenates at conditions (pH and ionic strength) similar to the physiological ones. Light scattering data were collected at two temperatures, 20 oC and 37 oC, over a wide range of concentrations from the very dilute limit up to the dense regime approaching to the physiological lens concentration. A comparison with experimental data from intact bovine lenses was advanced revealing differences between dispersions and lenses at similar concentrations. In the dilute regime two scattering entities were detected and identified with the long-time, self-diffusion modes of alpha-crystallins and their aggregates, which naturally exist in lens nucleus. Self-diffusion coefficients are temperature insensitive, whereas the collective diffusion coefficient depends strongly on temperature revealing a reduction of the net repulsive interparticle forces with lowering temperature. While there are no rigorous theoretical approaches on particle diffusion properties for multi-component, non-ideal hard-sphere, polydispersed systems, as the suspensions studied here, a discussion of the volume fraction dependence of the long-time, self-diffusion coefficient in the context of existing theoretical approaches was undertaken. This study is purported to provide some insight into the complex light scattering pattern of intact lenses and the interactions between the constituent proteins that are responsible for lens transparency. This would lead to understand basic mechanisms of specific protein interactions that lead to lens opacification (cataract) under pathological conditions.

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