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首页> 外文期刊>Biochemistry >Oligomerization and phase transitions in aqueous solutions of native and truncated human betaB1-crystallin.
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Oligomerization and phase transitions in aqueous solutions of native and truncated human betaB1-crystallin.

机译：天然和截短的人βB1晶状蛋白的水溶液中的低聚和相变。

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Human betaB1-crystallin is a major eye-lens protein that undergoes in vivo truncation at the N-terminus with aging. By studying native betaB1 and truncated betaB1DeltaN41, which mimics an age-related in vivo truncation, we have determined quantitatively the effect of truncation on the oligomerization and phase transition properties of betaB1 aqueous solutions. The oligomerization studies show that the energy of attraction between the betaB1DeltaN41 proteins is about 10% greater than that of the betaB1 proteins. We have found that betaB1DeltaN41 aqueous solutions undergo two distinct types of phase transitions. The first phase transition involves an initial formation of thin rodlike assemblies, which then evolve to form crystals. The induction time for the formation of rodlike assemblies is sensitive to oligomerization. The second phase transition can be described as liquid-liquid phase separation (LLPS) accompanied by gelation within the protein-rich phase. We refer to this process as heterogeneous gelation. These two phase transitions are not observed in the case of betaB1 aqueous solutions. However, upon the addition of poly(ethylene glycol) (PEG), we observe heterogeneous gelation also for betaB1. Our PEG experiments allow us to estimate the difference in phase separation temperatures between betaB1 and betaB1DeltaN41. This difference is consistent with the increase in energy of attraction found in our oligomerization studies. Our work suggests that truncation is a cataractogenic modification since it favors protein condensation and the consequent formation of light scattering elements, and highlights the importance of the N-terminus of betaB1 in maintaining lens transparency.
机译：人betaB1晶状蛋白是一种主要的眼透镜蛋白，会随着衰老在N端进行体内截短。通过研究模拟与年龄相关的体内截短的天然betaB1和截短的betaB1DeltaN41，我们定量确定了截断对betaB1水溶液的低聚和相变特性的影响。寡聚研究表明，betaB1DeltaN41蛋白之间的吸引能量比betaB1蛋白高约10％。我们发现betaB1DeltaN41水溶液经历两种不同类型的相变。第一个相变涉及细棒状组件的初始形成，然后细化成晶体。形成棒状组件的诱导时间对低聚反应敏感。第二相变可以描述为液-液相分离（LLPS），伴随着蛋白质富集相内的凝胶化。我们将此过程称为异质凝胶化。在betaB1水溶液中未观察到这两个相变。但是，在添加聚乙二醇（PEG）后，我们也观察到了betaB1的异质凝胶化。我们的PEG实验使我们能够估计betaB1和betaB1DeltaN41之间的相分离温度之差。这种差异与我们的低聚研究中发现的吸引能增加是一致的。我们的工作表明，截短是一种白内障致病性修饰，因为它有助于蛋白质凝聚和随后形成的光散射元素，并突出了betaB1的N末端在保持晶状体透明性中的重要性。

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