Mass spectrometry approaches to monitor protein-drug interactions.
Recent advances in mass spectrometry-based approaches have enabled the investigation of drug-protein interactions in various ways including the direct detection of drug-target complexes, the examination of drug-induced changes in the target protein structure, and the monitoring of enzymatic target activity. Mass spectrometry-based proteomics methods also permit the unbiased analysis of changes in protein abundance and post-translational modifications induced by drug action. Finally, chemoproteomic affinity enrichment studies enable the deconvolution of drug targets under close to physiological conditions. This review provides an overview of current methods for the characterization of drug-target interactions by mass spectrometry and describes a protocol for chemoproteomic target binding studies using immobilized bioactive molecules.
Cellzome AG, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
Nico
N
Zinn
Carsten
C
Hopf
Gerard
G
Drewes
Marcus
M
Bantscheff
D000818:Animals; D018929:Cell Culture Techniques; D002846:Chromatography, Affinity; D041961:Deuterium Exchange Measurement; D004353:Drug Evaluation, Preclinical / Q000379:methods; D057075:Enzyme Assays; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D058990:Molecular Targeted Therapy; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D040901:Proteomics
D011506:Proteins