Measuring protein-ligand interactions using liquid sample desorption electrospray ionization mass spectrometry

Pengyuan Liu, Jiang Zhang, Carly N. Ferguson, Hao Chen, Joseph A. Loo

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


We have previously shown that liquid sample desorption electrospray ionization-mass spectrometry (DESI-MS) is able to measure large proteins and noncovalently bound protein complexes (to 150 kDa) (Ferguson et al., Anal. Chem. 2011, 83, 6468-6473). In this study, we further investigate the application of liquid sample DESI-MS to probe protein-ligand interactions. Liquid sample DESI allows the direct formation of intact protein-ligand complex ions by spraying ligands toward separate protein sample solutions. This type of "reactive" DESI methodology can provide rapid information on binding stiochiometry, selectivity, and kinetics, as demonstrated by the binding of ribonuclease A (RNaseA, 13.7 kDa) with cytidine nucleotide ligands and the binding of lysozyme (14.3 kDa) with acetyl chitose ligands. A higher throughput method for ligand screening by liquid sample DESI was demonstrated, in which different ligands were sequentially injected as a segmented flow for DESI ionization. Furthermore, supercharging to enhance analyte charge can be integrated with liquid sample DESI-MS, without interfering with the formation of protein-ligand complexes.

Original languageEnglish (US)
Pages (from-to)11966-11972
Number of pages7
JournalAnalytical Chemistry
Issue number24
StatePublished - Dec 17 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry


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