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

  • Author(s) / Creator(s)
  • 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
  • Subjects / Keywords
  • Type of Item
    Article (Published)
  • DOI
    https://doi.org/10.7939/R31J97M7F
  • License
    © 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
  • Link to related item
    http://doi.org/10.1007/s13361-011-0311-9