Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 1. Chip-based analysis.
The use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF) in concert with surface plasmon resonance-based biomolecular interaction analysis (SPR-BIA) is reported. A chip-based biosensor unit was used to simultaneously monitor biomolecular interactions taking place on four different regions of the sensor chip (flow cells). Species retained during SPR-BIA were then identified by performing MALDI-TOF directly from within the area of the flow cells. Analyses were performed on an antibody/antigen/antibody system with detection limits in the low-femtomole range. The combined assay demonstrates the use of SPR-BIA to evaluate the relative stability of sequential solution-phase interactions, as well as, upon MALDI-TOF analysis, the ability to unambiguously confirm the presence of species retained during the interaction analysis.
Nelson
R W
RW
Department of Chemistry and Biochemistry, Arizona State University, Tempe 85287-1604, USA.
Krone
J R
JR
Jansson
O
O
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000937:Antigen-Antibody Reactions; D015374:Biosensing Techniques; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D009211:Myoglobin / Q000276:immunology; D011817:Rabbits; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D000911:Antibodies, Monoclonal; D007074:Immunoglobulin G; D009211:Myoglobin