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Issue 11, 2012
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Mass spectrometry based tools to investigate protein–ligand interactions for drug discovery

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Abstract

The initial stages of drug discovery are increasingly reliant on development and improvement of analytical methods to investigate protein–protein and protein–ligand interactions. For over 20 years, mass spectrometry (MS) has been recognized as providing a fast, sensitive and high-throughput methodology for analysis of weak non-covalent complexes. Careful control of electrospray ionization conditions has enabled investigation of the structure, stability and interactions of proteins and peptides in a solvent free environment. This critical review covers the use of mass spectrometry for kinetic, dynamic and structural studies of proteins and protein complexes. We discuss how conjunction of mass spectrometry with related techniques and methodologies such as ion mobility, hydrogen–deuterium exchange (HDX), protein footprinting or chemical cross-linking can provide us with structural information useful for drug development. Along with other biophysical techniques, such as NMR or X-ray crystallography, mass spectrometry provides a powerful toolbox for investigation of biological problems of medical relevance (204 references).

Graphical abstract: Mass spectrometry based tools to investigate protein–ligand interactions for drug discovery

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Publication details

The article was received on 05 Feb 2012 and first published on 24 Apr 2012


Article type: Critical Review
DOI: 10.1039/C2CS35035A
Citation: Chem. Soc. Rev., 2012,41, 4335-4355
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    Mass spectrometry based tools to investigate protein–ligand interactions for drug discovery

    K. J. Pacholarz, R. A. Garlish, R. J. Taylor and P. E. Barran, Chem. Soc. Rev., 2012, 41, 4335
    DOI: 10.1039/C2CS35035A

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