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首页> 外文期刊>Mass Spectrometry Reviews >NOVEL INSIGHTS INTO PROTEIN MISFOLDING DISEASES REVEALED BY ION MOBILITY-MASS SPECTROMETRY
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NOVEL INSIGHTS INTO PROTEIN MISFOLDING DISEASES REVEALED BY ION MOBILITY-MASS SPECTROMETRY

机译：离子淌度质谱显示了对蛋白质错售疾病的新见解

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摘要

Amyloid disorders incorporate a wide range of human diseases arising from the failure of a specific peptide or protein to adopt, or remain in, its native functional conformational state. These pathological conditions, such as Parkinson's disease, Alzheimer's disease and Huntington's disease are highly debilitating, exact enormous costs on both individuals and society, and are predicted to increase in prevalence. Consequently, they form the focus of a topical and rich area of current scientific research. A major goal in attempts to understand and treat protein misfolding diseases is to define the structures and interactions of protein species intermediate between fully folded and aggregated, and extract a description of the aggregation process. This has proven a difficult task due to the inability of traditional structural biology approaches to analyze structurally heterogeneous systems. Continued developments in instrumentation and analytical approaches have seen ion mobility-mass spectrometry (IM-MS) emerge as a complementary approach for protein structure determination, and in some cases, a structural biology tool in its own right. IM-MS is well suited to the study of protein mis-folding, and has already yielded significant structural information for selected amyloidogenic systems during the aggregation process. This review describes IM-MS for protein structure investigation, and provides a summary of current research highlighting how this methodology has unequivocally and unprece-dentedly provided structural and mechanistic detail pertaining to the oligomerization of a variety of disease related proteins.
机译：淀粉样蛋白疾病包括由于特定肽或蛋白质无法采用或保持其天然功能构象状态而引起的多种人类疾病。这些病理状况，如帕金森氏病，阿尔茨海默氏病和亨廷顿氏病，极易使人衰弱，给个人和社会造成巨大的代价，并预计患病率会增加。因此，它们构成了当前科学研究领域的热点和重点。试图了解和治疗蛋白质错误折叠疾病的主要目标是定义介于完全折叠和聚集之间的蛋白质种类的结构和相互作用，并提取聚集过程的描述。由于传统的结构生物学方法无法分析结构异质的系统，这已被证明是一项艰巨的任务。仪器和分析方法的不断发展已使离子淌度质谱（IM-MS）成为蛋白质结构测定的一种补充方法，在某些情况下，它本身就是一种结构生物学工具。 IM-MS非常适合蛋白质错折叠的研究，并且在聚集过程中已经为选定的淀粉样蛋白生成系统提供了重要的结构信息。这篇综述描述了用于蛋白质结构研究的IM-MS，并提供了当前研究的摘要，突出了这种方法如何毫不含糊地提供与各种疾病相关蛋白质寡聚化有关的结构和机理的详细信息。

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