Journal
ANALYTICAL CHEMISTRY
Volume 85, Issue 24, Pages 11966-11972Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac402906d
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Funding
- National Science Foundation [CHE-0911160]
- NSF Career [CHE-1149367]
- ASMS Research Award (Thermo Scientific)
- National Natural Science Foundation of China (NNSFC) [21328502]
- Ruth L. Kirschstein National Research Service Award [GM007185]
- National Institutes of Health [R01 GM103479]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1149367] Funding Source: National Science Foundation
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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.
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