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Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions

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Abstract

Ion mobility–mass spectrometry (IM-MS) is a powerful tool for the simultaneous analysis of mass, charge, size, and shape of ionic species. It allows the characterization of even low-abundant species in complex samples and is therefore particularly suitable for the analysis of proteins and their assemblies. In the last few years even complex and intractable species have been investigated successfully with IM-MS and the number of publications in this field is steadily growing. This trend article highlights recent advances in which IM-MS was used to study protein–ligand complexes and in particular focuses on the catch and release (CaR) strategy and collision-induced unfolding (CIU).

Native mass spectrometry and ion mobility-mass spectrometry are versatile tools to follow the stoichiometry, energetics, and structural impact of protein-ligand binding.

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Acknowledgments

Melanie Göth thanks Bayer Pharma AG for funding a PhD fellowship. The authors acknowledge Dr. Oren Moscovitz and Dr. Benno Kuropka for critical reading of the manuscript.

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Authors and Affiliations

  1. Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 3, 14195, Berlin, Germany

    Melanie Göth & Kevin Pagel

  2. Department of Molecular Physics, Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany

    Melanie Göth & Kevin Pagel

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  1. Melanie Göth
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Correspondence to Kevin Pagel.

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Göth, M., Pagel, K. Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions. Anal Bioanal Chem 409, 4305–4310 (2017). https://doi.org/10.1007/s00216-017-0384-9

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