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

Analytical and Bioanalytical Chemistry
Melanie Göth, Kevin Pagel

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). Graphical Abstract 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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Citations

Feb 17, 2018·Journal of the American Society for Mass Spectrometry·Bradley B Stocks, Jeremy E Melanson
Aug 3, 2018·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Christopher KuneEdwin De Pauw
Jul 15, 2020·Journal of Mass Spectrometry : JMS·Marie Barth, Carla Schmidt
Oct 13, 2017·Journal of Separation Science·Valentina D'AtriDavy Guillarme
Jan 18, 2020·Journal of the American Society for Mass Spectrometry·Lucienne NouchikianDerek J Wilson
Sep 21, 2017·Journal of the American Chemical Society·Tae Su ChoiHugh I Kim
Aug 21, 2021·Chemical Reviews·Sem TamaraAlbert J R Heck
Aug 28, 2021·Chemical Reviews·Jack L BennettWilliam A Donald

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