Capture and analysis of low molecular weight ligands by surface plasmon resonance combined with mass spectrometry

01 January 2001

Sönksen, C.P., Markgren, P.-O., Hämäläinen, M., Jansson, Ö., Danielson, U.H. and Roepstorff, P. (2001) European Journal of Mass Spectrometry 7, 385-391.

The combination of surface plasmon resonance (SPR) and mass spectrometry (MS) has created a unique approach to protein investigations. Surface plasmon resonance is used to quantify interactions between proteins and surface-immobilized ligands, and MS is used to determine the structural features of the bound proteins. Recent progress in SPR–MS includes improved methods and operations, increased limits of detection, multi-protein analysis and protein-complex delineation. With the subsequent design of SPR protein arrays, SPR–MS is expected to enter into the field of high-throughput protein interaction discovery and miniaturized diagnostics.

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