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.
Text
Vonderach et al 2017 v4 ref_clean.docx - Author Accepted Manuscript Download (851kB) |
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 |
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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: | |
URI: | https://livrepository.liverpool.ac.uk/id/eprint/3015716 |