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Oral Sessions
Day 4, June 25（Wed.） 11:40-11:55
Room B (Maesato Center)
- 4B-O1-1140（2P-PM-33）
Investigation of ligand transfer mechanism during collisional activation of protein complexes in native mass spectrometry
(Zhejiang Univ.)
oShiwen Zhou, Mowei Zhou, Hongru Feng, Yuanjiang Pan
Native mass spectrometry (native MS) is a valuable tool for studying protein-ligand and protein-metal interactions. This study investigates the collisional activation mechanisms—collision-induced dissociation (CID) and surface-induced dissociation (SID)—of the nsp10/16 complex from SARS-CoV-2, a crucial enzyme complex involved in viral RNA synthesis. Previous study shows the Nsp10 can enhance the 2-O-MTase activity of nsp16, and understanding their interaction could aid antiviral drug development. We explore how CID and SID influence the dissociation and structural dynamics of nsp10/16, focusing on zinc ion transfer between the subunits. Preliminary results indicate that CID induces zinc transfer from nsp10 to nsp16, while SID maintains zinc binding within nsp10. Ion mobility spectrometry also provides insights into the structural changes during dissociation. Additionally, the charge state of the nsp10/16 dimer influences the degree of dissociation. In negative ion mode, a smaller proportion of zinc is transferred, while in positive ion mode, the extent of zinc transfer is dependent on the CID collision energy. To deepen our understanding, we employ native-top down MS to correlate solution-phase and gas-phase structures, providing new insights into the function of zinc in non-structural proteins. This work enhances the interpretation of native MS data for other protein-ligand and protein-metal complexes, contributing to drug discovery efforts.