Biosensor chip mass spectrometry: A chip-based proteomics approach

Rapid advances in genomic sequencing, bioinformatics, and analytical instru mentation have created the field of proteomics, which at present is based l argely on two-dimensional electrophoresis (2-DE) separation of complex prot ein mixtures and identification of individual proteins using mass spectrome try. These analyses provide a wealth of data, which upon further evaluation leads to many questions regarding the structure and function of the protei ns. The challenge of answering these questions create a need for high-speci ficity approaches that may be used in the analysis of biomolecular recognit ion events and interacting partners, and thereby places great demands on ge neral protein characterization instrumentation and the types of analyses th ey need to perform. Over the past five years we have been actively involved in interfacing two general, instrumental techniques, surface plasmon reson ance-biomolecular interaction analysis (SPR-BIA) and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry, into a single concerted approach for use in the functional and structural characte rization of proteins. Reviewed here is the recent progress made using biomo lecular interaction analysis - mass spectrometry (BIA-MS) in the detailed c haracterization of proteins and protein-protein interactions and the develo pment of biosensor chip mass spectrometry (BCMS) as a new chip-based proteo mics approach.