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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Exploring the Aggregation Propensity of γS-Crystallin Protein Variants Using Two-Dimensional Spectroscopic Tools
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Exploring the Aggregation Propensity of γS-Crystallin Protein Variants Using Two-Dimensional Spectroscopic Tools

机译：使用二维光谱学工具探索γS-晶体蛋白变体的聚集倾向

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摘要

The formation of amyloid fibrils is associated with many serious diseases as well as diverse biological functions. Despite the importance of these aggregates, predicting the aggregation propensity of a particular sequence is a major challenge. We report a joint 2D nuclear magnetic resonance (NMR) and ultraviolet (2DUV) study of fibrillization in the wild-type and two aggregation-prone mutants of the eye lens protein γS-crystallin. Simulations show that the complexity of 2DUV signals as measured by their "approximate entropy" is a good indicator for the conformational entropy and in turn is strongly correlated with its aggregation propensity. These findings are in agreement with high-resolution NMR experiments and are corroborated for amyloid fibrils. The 2DUV technique is complementary to high-resolution structural methods and has the potential to make the evaluation of the aggregation propensity for protein variant propensity of protein structure more accessible to both theory and experiment. The approximate entropy of experimental 2DUV signals can be used for fast screening, enabling identification of variants with high fibrillization propensity for the much more time-consuming NMR structural studies, potentially expediting the characterization of protein variants associated with cataract and other protein aggregation diseases.
机译：淀粉样蛋白原纤维的形成与许多严重的疾病以及多种生物学功能有关。尽管这些聚集体很重要，但是预测特定序列的聚集倾向仍是一个重大挑战。我们报告了联合的二维核磁共振（NMR）和紫外线（2DUV）研究在晶状体蛋白γS-crystallin的野生型和两个易于聚集的突变体中的原纤维化。仿真表明，通过2DUV信号的“近似熵”测量的复杂度是构象熵的良好指标，并且反过来又与其聚集倾向紧密相关。这些发现与高分辨率的NMR实验一致，并证实了淀粉样蛋白原纤维。 2DUV技术是高分辨率结构方法的补充，具有使蛋白质结构的蛋白质变异倾向的聚集倾向评估更容易从理论和实验上获得的潜力。实验2DUV信号的近似熵可用于快速筛选，从而能够鉴定出具有较高原纤维化倾向的变体，以进行更耗时的NMR结构研究，从而有可能加快与白内障和其他蛋白质聚集疾病相关的蛋白质变体的表征。

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