Surface plasmon resonance/mass spectrometry interface.
A strategy for combining surface plasmon resonance (SPR) biomolecular interaction analysis, and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is reported. Both techniques are highly complementary but need separate optimization to improve their individual specificity and sensitivity. Sensor surfaces that are optimal for kinetic analysis are not well suited for MALDI-MS and vice versa. In addition, the transfer of analyte from SPR to MS is crucial and often accompanied by sample loss. To address both of these points, a bifunctional SPR fluid cell was constructed where optimized surfaces can be used for binding studies and MS simultaneously with regard to the special need of each technique. The setup guarantees that the SPR and the loading experiment for MS are performed at identical conditions. A removable pin carries the affinity-surface-bound analyte to the mass spectrometer so that handling is minimized, avoiding analyte elution. Functionalized transfer pins can also be used independently of SPR for microaffinity capture-MS.
Grote
Jens
J
Integrated Functional Genomics, Interdisciplinary Center for Clinical Research, Medical Faculty, University of Muenster, Roentgenstrasse 21, 48149 Muenster, Germany.
Dankbar
Nico
N
Gedig
Erk
E
Koenig
Simone
S
D015374:Biosensing Techniques; D045304:Cytochromes c / Q000032:analysis; D020100:Hydrogels; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D020349:Surface Plasmon Resonance / Q000379:methods*
D020100:Hydrogels; D045304:Cytochromes c