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Ion mobility-mass spectrometry and orthogonal gas-phase techniques to study amyloid formation and inhibition

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Hoffmann,  Waldemar
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Institute of Chemistry and Biochemistry, Freie Universität Berlin;

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Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Institute of Chemistry and Biochemistry, Freie Universität Berlin;

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Hoffmann, W., Helden, G. v., & Pagel, K. (2017). Ion mobility-mass spectrometry and orthogonal gas-phase techniques to study amyloid formation and inhibition. Current Opinion in Structural Biology, 46, 7-15. doi:10.1016/j.sbi.2017.03.002.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-9491-3
Abstract
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.