Surface Plasmon Resonance Biomolecular Interaction Analysis Mass Spectrometry. 1. Chip-Based Analysis

• Published in: Analytical chemistry (Washington) Vol. 69; no. 21; pp. 4363 - 4368
• Main Authors: Nelson, Randall W, Krone, Jennifer R, Jansson, Osten
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-11-1997
• Subjects: Animals; Antibodies, Monoclonal - immunology; Antigen-Antibody Reactions; Biological and medical sciences; Biosensing Techniques; Fundamental and applied biological sciences. Psychology; Humans; Immunoglobulin G - immunology; Interactions. Associations; Intermolecular phenomena; Molecular biophysics; Myoglobin - immunology; Rabbits; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods; Investigation method; Model study; Molecular interaction; Surface plasmon; Chip; Mass spectrometry; Laser desorption; Chemical ionization; Immune complex
• ISSN: 0003-2700; 1520-6882
• DOI: 10.1021/ac970538w

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.