Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, Berlin 14195, Germany; Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, Berlin 14195, Germany.
Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, Berlin 14195, Germany.
Curr Opin Struct Biol. 2017 Oct;46:7-15. doi: 10.1016/j.sbi.2017.03.002. Epub 2017 Mar 23.
Amyloidogenic peptide oligomers are responsible for a variety of neurodegenerative disorders such as Alzheimer's and Parkinson's disease. Due to their dynamic, polydisperse, and polymorphic nature, these oligomers are very challenging to characterize using traditional condensed-phase methods. In the last decade, ion mobility-mass spectrometry (IM-MS) and related gas-phase techniques have emerged as a powerful alternative to disentangle the structure and assembly characteristics of amyloid forming systems. This review highlights recent advances in which IM-MS was used to characterize amyloid oligomers and their underlying assembly pathway. In addition, we summarize recent studies in which IM-MS was used to size- and mass-select species for a further spectroscopic investigation and outline the potential of IM-MS as a tool for the screening of amyloid inhibitors.
淀粉样肽寡聚体是多种神经退行性疾病（如阿尔茨海默病和帕金森病）的罪魁祸首。由于其动态、多分散和多态性，使用传统的凝聚相方法对这些寡聚体进行特征描述非常具有挑战性。在过去的十年中，离子淌度-质谱（IM-MS）和相关的气相技术已经成为一种强大的替代方法，可以解析淀粉样形成系统的结构和组装特征。本综述重点介绍了最近利用 IM-MS 来表征淀粉样寡聚体及其潜在组装途径的进展。此外，我们还总结了最近利用 IM-MS 对物种进行大小和质量选择以进行进一步光谱研究的研究，并概述了 IM-MS 作为淀粉样抑制剂筛选工具的潜力。
