Fast Protein Footprinting by X-ray Mediated Radical Trifluoromethylation
Ming Cheng, Awuri Asuru, Janna Kiselar, M. George, Mark R. Chance, Michael L. Gross
Abstract
Synchrotron radiolysis generates hydroxyl radicals (•OH) that are successful footprinting reagents. Here, we describe a new reagent for the synchrotron platform, the trifluoromethyl radical (•CF3). The radical is produced by •OH displacement of •CF3 from sodium triflinate (Langlois reagent). Upon X-ray beam exposure, the reagent labels proteins extensively without any additional chemicals on a millisecond or shorter time scale. The •CF3 is comparably reactive to •OH and produces footprinting information that complements that of •OH alone. This reagent in combination with •OH should enable novel chemistry for protein footprinting on the synchrotron platform.
Topics & Concepts
ChemistryReagentFootprintingRadicalSynchrotronTrifluoromethylationTrifluoromethylCombinatorial chemistryPhotochemistryOrganic chemistryBiochemistryAlkylTranscription factorNuclear physicsPhysicsGeneFluorine in Organic ChemistryChemical Synthesis and AnalysisMass Spectrometry Techniques and Applications