title: Fast photochemical oxidation of proteins for epitope mapping.
abstract: The growing use of monoclonal antibodies as therapeutics underscores the importance of epitope mapping as an essential step in characterizing antibody-antigen complexes. The use of protein footprinting coupled with mass spectrometry, which is emerging as a tool in structural biology, offers opportunities to map antibody-binding regions of antigens. We report here the use of footprinting via fast photochemical oxidation of proteins (FPOP) with OH radicals to characterize the epitope of the serine protease thrombin. The data correlate well with previously published results that determined the epitope of thrombin. This study marks the first time oxidative labeling has been used for epitope mapping.
authors: Department of Chemistry, Washington University, St. Louis, Missouri 63130, USA. lmjones@wustl.edu
authors: Lisa M
authors: LM
authors: Jones
authors: Justin
authors: J
authors: B Sperry
authors: James
authors: J
authors: A Carroll
authors: Michael L
authors: ML
authors: Gross
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology*; D000936:Antigen-Antibody Complex; D002851:Chromatography, High Pressure Liquid; D018604:Epitope Mapping / Q000379:methods*; D017665:Hydroxyl Radical / Q000737:chemistry; D013058:Mass Spectrometry; D010084:Oxidation-Reduction; D013917:Thrombin / Q000276:immunology* / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D017665:Hydroxyl Radical; D014357:Trypsin; D013917:Thrombin