Understanding protein-drug interactions using ion mobility-mass spectrometry

Eyers, Claire E ORCID: 0000-0002-3223-5926, Vonderach, Matthias, Ferries, Samantha, Jeacock, Kiani and Eyers, Patrick A ORCID: 0000-0002-9220-2966 (2018) Understanding protein-drug interactions using ion mobility-mass spectrometry. CURRENT OPINION IN CHEMICAL BIOLOGY, 42. pp. 167-176.

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Abstract

Ion mobility-mass spectrometry (IM-MS) is an important addition to the analytical toolbox for the structural evaluation of proteins, and is enhancing many areas of biophysical analysis. Disease-associated proteins, including enzymes such as protein kinases, transcription factors exemplified by p53, and intrinsically disordered proteins, including those prone to aggregation, are all amenable to structural analysis by IM-MS. In this review we discuss how this powerful technique can be used to understand protein conformational dynamics and aggregation pathways, and in particular, the effect that small molecules, including clinically-relevant drugs, play in these processes. We also present examples of how IM-MS can be used as a relatively rapid screening strategy to evaluate the mechanisms and conformation-driven aspects of protein:ligand interactions.

Item Type:	Article
Uncontrolled Keywords:	Humans, Protein Kinases, Proteins, Pharmaceutical Preparations, Ligands, Molecular Structure, Protein Conformation, Protein Binding, Mass Spectrometry, Intrinsically Disordered Proteins, Ion Mobility Spectrometry
Depositing User:	Symplectic Admin
Date Deposited:	09 Jan 2018 14:08
Last Modified:	19 Jan 2023 06:46
DOI:	10.1016/j.cbpa.2017.12.013
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3015716