Abstract
This method describes the combination of chemical cross-linking and high-resolution mass spectrometry for analyzing conformational changes in target proteins that are induced by drug binding. Our approach is exemplified for detecting conformational changes within the peroxisome proliferator-activated receptor alpha upon binding of low-molecular weight compounds, proving that our strategy provides a basis to efficiently characterize target protein–drug interactions.
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Acknowledgments
MQM is supported by the DFG-funded Graduiertenkolleg 1026 at the Martin-Luther-Universität Halle-Wittenberg. Dr. C. Ihling is acknowledged for valuable advice and assistance on the nano-HPLC/nano-ESI-MS system.
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Müller, M.Q., Sinz, A. (2012). Chemical Cross-Linking and High-Resolution Mass Spectrometry to Study Protein–Drug Interactions. In: Drewes, G., Bantscheff, M. (eds) Chemical Proteomics. Methods in Molecular Biology, vol 803. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-364-6_14
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