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Poster Presentations
Day 4, June 25（Wed.）
Room P (Maesato East, Foyer, Ocean Wing)
- 4P-PM-27
Single-cell native mass spectrometry of cultured human cells for characterization of protein non-covalent interactions
(Yokohama City Univ.)
Noa Suzuki, Yuko Inatomi, oMichiko Tajiri, Tsuyoshi Konuma, Satoko Akashi
Native mass spectrometry (MS) is a technique that enables the direct observation of non-covalent protein interactions. Typically, native MS samples are separated, purified, and prepared in volatile solutions. However, the intracellular environment is highly crowded, containing 20–40 wt% proteins, cellular organelles, and other macromolecules. In such a setting, biomolecular interactions often differ from those observed in vitro, and drugs optimized for in vitro conditions may not exhibit the expected efficacy in cells.
To accurately assess biomolecular and drug interactions within living cells, it is important to analyze proteins under conditions that closely mimic the intracellular environment, without isolation and purification.
We have therefore developed single-cell native MS to investigate non-covalent protein interactions at the single-cell level by modifying Masujima's “live single-cell MS" method. Using this approach, we successfully ditected intact tetrameric hemoglobin from a single red blood cell by native MS. This is the first successful demonstration of single-cell native MS worldwide. We then extended this method to cultured human cells (HEK293T). In this presentation, we report its application to HEK293T cells overexpressing target proteins, enabling the direct detection of intact proteins and protein-ligand complexes in single cells using native mass spectrometry.