One of our key goals is the translation of targeted MS-based assays for proteins and small molecules into the clinic. This will allow for more sensitive and precise early detection of diseases, better treatment optimization, and an improved therapeutic monitoring.
We develop specific Multiple Reaction Monitoring mass spectrometry (MRM-MS) assays for quantifying small molecules in blood and plasma in close collaboration with clinicians at the Jewish General Hospital.
1. Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma. Kuzyk, M.A., Smith, D., Yang, J., Cross, T.J., Jackson, A.M., Hardie, D.B., Anderson, N.L., Borchers, C.H., 2009. Mol. Cell. Proteomics MCP 8, 1860–1877.
2. MRM-based multiplexed quantitation of 67 putative cardiovascular disease biomarkers in human plasma. Domanski, D., Percy, A.J., Yang, J., Chambers, A.G., Hill, J.S., Freue, G.V.C., Borchers, C.H., 2012. Proteomics 12, 1222–1243.
We furthermore develop immuno-MALDI (iMALDI) assays for the highly sensitive, specific and automated quantification of proteins and their phosphorylation states from cells, fresh-frozen tissues and FFPE tissues. The workflow includes the extraction of proteins, enzymatic digestion, the spike-in of stable isotope-labeled reference standard (SIS) peptides, and the combined immunocapture of the endogenous peptide and its SIS counterpart. The signal is measured by MALDI-MS, allowing the absolute quantification of proteins. As the workflow requires no LC system and can be fully automated, it represents a promising technology to precisely quantify proteins from minimal sample amounts such as needle biopsies with the robustness required for a real clinical setting.
1. How iMALDI can improve clinical diagnostics. Popp, R., Basik, M., Spatz, A., Batist, G., Zahedi, R.P., Borchers, C.H., 2018.
Clin. Chem. 64, 1271–1272.
2. Immuno-MALDI-TOF-MS in the Clinic. Zahedi, R.P., Parker, C.E., Borchers, C.H., 2018.