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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet? Open Access

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Author or creator
Kitova, Elena N.
El-Hawiet, Amr
Schnier, Paul D.
Klassen, John S.
Additional contributors
Subject/Keyword
Electrospray ionization mass spectrometry
Binding assay
Library screening
Protein-ligand interaction
Association constant
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete understanding of biochemical reactions and pathways and to the design of novel therapeutic agents that may be used to treat a variety of diseases and infections. Over the last 20 y, electrospray ionization mass spectrometry (ESI-MS) has emerged as a versatile tool for the identification and quantification of protein–ligand interactions in vitro. Here, we describe the implementation of the direct ESI-MS assay for the determination of protein–ligand binding stoichiometry and affinity. Additionally, we outline common sources of error encountered with these measurements and various strategies to overcome them. Finally, we comment on some of the outstanding challenges associated with the implementation of the assay and highlight new areas where direct ESI-MS measurements are expected to make significant contributions in the future.
Date created
2012
DOI
doi:10.7939/R31J97M7F
License information
© 2012 Kitova, E. N., El-Hawiet, A., Schnier, P. D., & Klassen, J. S. This version of this article is open access and can be downloaded and shared. The original author(s) and source must be cited.
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Citation for previous publication
Kitova, E. N., El-Hawiet, A., Schnier, P. D., & Klassen, J. S. (2012). Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet? Journal of the American Society for Mass Spectrometry, 23(3), 431-441.  http://doi.org/10.1007/s13361-011-0311-9

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