Kinetic and thermodynamic stability of bacterial intracellular aggregates
Kinetic and thermodynamic stability of bacterial intracellular aggregates
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DOI：
10.1016/j.febslet.2008.09.049
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发表时间：
2008-10-29
期刊：
影响因子：
3.5
通讯作者：
Ventura, Salvador
中科院分区：
文献类型：
--
作者：
Espargaro, Alba;Sabate, Raimon;Ventura, Salvador
蛋白质聚集与许多人类疾病有关，是蛋白质生产的主要瓶颈。然而，人们对体内形成的聚集体的构象性质以及它们与嵌入其中的特定多肽的关系知之甚少。在这里，我们发现A β 42阿尔茨海默肽及其Asp19异体形成的包涵体的动力学和热力学稳定性存在显著差异，并与它们在细胞内的淀粉样变性倾向和溶解度相关。我们的研究结果表明，多肽链的性质决定了细胞内聚集体的特定构象性质。这意味着不同的蛋白质内含物对细胞质量控制机制施加了不同的挑战。(c) 2008年欧洲生化学会联合会。Elsevier b.v.版权所有。
Protein aggregation is related to many human disorders and constitutes a major bottleneck in protein production. However, little is known about the conformational properties of in vivo formed aggregates and how they relate to the specific polypeptides embedded in them. Here, we show that the kinetic and thermodynamic stability of the inclusion bodies formed by the A beta 42 Alzheimer peptide and its Asp19 alloform differ significantly and correlate with their amyloidogenic propensity and solubility inside the cell. Our results indicate that the nature of the polypeptide chain determines the specific conformational properties of intracellular aggregates. This implies that different protein inclusions impose dissimilar challenges to the cellular quality-control machinery. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.