SPR-MS in functional proteomics.
The mapping of protein networks and the establishment of the functional relationships between expressed proteins and their effects on cellular processes represents a great challenge for functional or interaction proteomics. The combination of surface plasmon resonance (SPR)-based technology with mass spectrometry (MS) has created a unique analytical tool for functional proteomics investigations. Proteins are affinity purified, quantified and characterised in terms of their interactions, while the mass spectrometer identifies and structurally characterises the biomolecules. Recent developments have led to a closer integration of these key technologies, providing a combined approach which enables identification of proteins selected on the basis of their functional binding criteria. In addition to a historical overview of this field, some recent detailed examples of combined SPR-MS approaches will be reviewed in a number of key application areas, including ligand fishing, peptide sequence and post-translational modification analysis by SPR-MS/MS and enzyme inhibitor screening.
Buijs
Jos
J
Biacore AB, Rapsgatan 7, 754 50 Uppsala, Sweden. Jos.Buijs@Biacore.com
Franklin
Gary C
GC
D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D008024:Ligands; D013058:Mass Spectrometry / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D020349:Surface Plasmon Resonance / Q000379:methods*
D004791:Enzyme Inhibitors; D008024:Ligands; D010455:Peptides