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      Developments in tandem ion mobility mass spectrometry

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          Abstract

          Ion Mobility (IM) coupled to mass spectrometry (MS) is a useful tool for separating species of interest out of small quantities of heterogenous mixtures via a combination of m/z and molecular shape. While tandem MS instruments are common, instruments which employ tandem IM are less so with the first commercial IM–MS instrument capable of multiple IM selection rounds being released in 2019. Here we explore the history of tandem IM instruments, recent developments, the applications to biological systems and expected future directions.

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          Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease.

          Summer Bernstein, Nicholas Dupuis, Noel Lazo … (2009)
          In recent years, small protein oligomers have been implicated in the aetiology of a number of important amyloid diseases, such as type 2 diabetes, Parkinson's disease and Alzheimer's disease. As a consequence, research efforts are being directed away from traditional targets, such as amyloid plaques, and towards characterization of early oligomer states. Here we present a new analysis method, ion mobility coupled with mass spectrometry, for this challenging problem, which allows determination of in vitro oligomer distributions and the qualitative structure of each of the aggregates. We applied these methods to a number of the amyloid-β protein isoforms of Aβ40 and Aβ42 and showed that their oligomer-size distributions are very different. Our results are consistent with previous observations that Aβ40 and Aβ42 self-assemble via different pathways and provide a candidate in the Aβ42 dodecamer for the primary toxic species in Alzheimer's disease.
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            Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process

            Roman A. Zubarev, Neil Kelleher, Fred W. McLafferty (1998)
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              Applications of a travelling wave-based radio-frequency-only stacked ring ion guide.

              Kevin Giles, Steven Pringle, Kenneth R Worthington … (2004)
              The use of radio-frequency (RF)-only ion guides for efficient transport of ions through regions of a mass spectrometer where the background gas pressure is relatively high is widespread in present instrumentation. Whilst multiple collisions between ions and the background gas can be beneficial, for example in inducing fragmentation and/or decreasing the spread in ion energies, the resultant reduction of ion axial velocity can be detrimental in modes of operation where a rapidly changing influx of ions to the gas-filled ion guide needs to be reproduced at the exit. In general, the RF-only ion guides presently in use are based on multipole rod sets. Here we report investigations into a new mode of ion propulsion within an RF ion guide based on a stack of ring electrodes. Ion propulsion is produced by superimposing a voltage pulse on the confining RF of an electrode and then moving the pulse to an adjacent electrode and so on along the guide to provide a travelling voltage wave on which the ions can surf. Through appropriate choice of the travelling wave pulse height, velocity and gas pressure it will be shown that the stacked ring ion guide with the travelling wave is effective as a collision cell in a tandem mass spectrometer where fast mass scanning or switching is required, as an ion mobility separator at pressures around 0.2 mbar, as an ion delivery device for enhancement of duty cycle on an orthogonal acceleration time-of-flight (oa-TOF) mass analyser, and as an ion fragmentation device at higher wave velocities. 2004 John Wiley & Sons, Ltd.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Biochem Soc Trans
                Journal ID (iso-abbrev): Biochem Soc Trans
                Journal ID (publisher-id): BST
                Title: Biochemical Society Transactions
                Publisher: Portland Press Ltd.
                ISSN (Print): 0300-5127
                ISSN (Electronic): 1470-8752
                Publication date (Print): 18 December 2020
                Publication date (Electronic): 18 December 2020
                Volume: 48
                Issue: 6
                Pages: 2457-2466
                Affiliations
                [1 ]Institute of Structural and Molecular Biology, UCL, Gower St, London WC1E 6BT, U.K.
                [2 ]Institute of Structural and Molecular Biology, Birkbeck University, Malet Place, London WC1E 7HX, U.K.
                Author notes
                Correspondence: Konstantinos Thalassinos ( k.thalassinos@ 123456ucl.ac.uk )
                Author information
                https://orcid.org/0000-0001-5306-3644
                http://orcid.org/0000-0001-5072-8428
                Article
                Publisher ID: BST-48-2457
                DOI: 10.1042/BST20190788
                PMC ID: 7752082
                PubMed ID: 33336686
                SO-VID: c78a8751-a8ef-4a90-b756-1095c4d84e2e
                Copyright © © 2020 The Author(s)
                License:

                This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY). Open access for this article was enabled by the participation of University College London in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with JISC.

                History
                Date received : 15 June 2020
                Date revision received : 14 October 2020
                Date accepted : 17 November 2020
                Categories
                Subject: Biophysics
                Subject: Structural Biology
                Subject: Review Articles

                ScienceOpen disciplines: Biochemistry
                Keywords: ion mobility,mass spectrometry,protein structure,tandem ion mobility
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: ion mobility, mass spectrometry, protein structure, tandem ion mobility

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