Direct ionization of large proteins and protein complexes by desorption electrospray ionization-mass spectrometry

Carly N. Ferguson, Sabrina A. Benchaar, Zhixin Miao, Joseph A. Loo, Hao Chen

Research output: Contribution to journalArticlepeer-review

92 Scopus citations


Desorption electrospray ionization-mass spectrometry (DESI-MS) has advantages for rapid sample analysis with little or no sample pretreatment, but performance for large biomolecules has not been demonstrated. In this study, liquid sample DESI, an extended version of DESI used for analysis of liquid samples, was shown to have capabilities for direct ionization of large noncovalent protein complexes (>45 kDa) and proteins (up to 150 kDa). Protein complex ions (e.g., superoxide dismutase, enolase, and hemoglobin) desorbed from solution by liquid sample DESI were measured intact, indicating the capability of DESI for preserving weak noncovalent interactions. Doping the DESI spray solvent with supercharging reagents resulted in protein complex ions having increased multiple charging without complex dissociation. Ion mobility measurements of model protein cytochrome c showed that the supercharging reagent favored the more compact conformation for the lower charged protein ions. Liquid sample DESI of hydrophobic peptide gramicidin D suggests that the ionization mechanism involves a droplet pick-up mixing process. Measurement of liquid samples significantly extends the mass range of DESI-MS, allowing the analysis of high-mass proteins such as 150 kDa immunoglobulin G (IgG) and thus represents the largest protein successfully ionized by DESI to date.

Original languageEnglish (US)
Pages (from-to)6468-6473
Number of pages6
JournalAnalytical Chemistry
Issue number17
StatePublished - Sep 1 2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry


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