Reduced Pressure Ionization Enhances Native Mass Spectrometry of Proteins and Protein Complexes.

ABSTRACT: Native mass spectrometry (MS) enables the analysis of protein interactions in complex biological mixtures. However, nonvolatile salts and buffers commonly present in such samples can cause ion adduction, peak broadening, and reduced signal intensity. Reducing the pressure surrounding the ionization emitter significantly improves native MS performance under these challenging conditions. Signal enhancements of up to 20-fold were observed with nanoscale emitters, and up to 7-fold with microscale emitters in high-salt solutions. Protein ions remained detectable in solutions containing up to 300 mM NaCl, unlike ambient pressure ionization. High signal-to-noise was observed for the DDB1:DCAF1 complex at 50 nM using reduced pressure ionization, whereas no readily assignable signal was detected at

SUBMITTER: Violi JP 

PROVIDER: S-EPMC12559447 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature