Understanding protein–drug interactions using ion mobility–mass spectrometry

Understanding protein–drug interactions using ion mobility–mass spectrometry 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Chemical Biology Elsevier

Understanding protein–drug interactions using ion mobility–mass spectrometry

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Publisher
Elsevier
Copyright
Copyright © 2018 The Authors
ISSN
1367-5931
D.O.I.
10.1016/j.cbpa.2017.12.013
Publisher site
See Article on Publisher Site

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.

Journal

Current Opinion in Chemical BiologyElsevier

Published: Feb 1, 2018

References

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