オーラルセッション
- 第1日 6月22日(水) 17:30~17:50 A会場(メインホール)
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1A-O1-1730 PDF
標的タンパク質同定に向けたヒスチジン重水素置換質量分析法の検討
It is known that binding of a ligand stabilizes proteins against chemical or heat-induced denaturation. Based on this principle, several mass spectrometry-based proteomic approaches for identifying protein-ligand interactions have been developed, such as SPROX (Stability of Proteins from Rates of Oxidation), DARTS (Drug Affinity Responsive Target Stability), CETSA (Cellular Thermal Shift Assay) and TPP (Thermal Proteome Profiling). Although these methods have shown encouraging results, identifying low abundant and multi-domain proteins is still a challenge. We foresee that histidine hydrogen-deuterium exchange mass spectrometry (His-HDX-MS), which measures the slow HDX of histidine imidazole groups in proteins using mass spectrometry, has the potential to overcome these drawbacks. Here we used His-HDX-MS as a platform to measure heat-induced unfolding of proteins and evaluated the applicability of this platform to identify protein-ligand interactions.