Reversed phase liquid chromatography hyphenated to continuous flow-extractive desorption electrospray ionization-mass spectrometry for analysis and charge state manipulation of undigested proteins
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
PubMed
26307717
DOI
10.1255/ejms.1364
Knihovny.cz E-resources
- MeSH
- Equipment Failure Analysis MeSH
- Chromatography, Reverse-Phase instrumentation MeSH
- Equipment Design MeSH
- Spectrometry, Mass, Electrospray Ionization instrumentation MeSH
- Specimen Handling instrumentation MeSH
- Peptide Mapping instrumentation MeSH
- Proteins analysis chemistry MeSH
- Static Electricity MeSH
- Chromatography, High Pressure Liquid instrumentation MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Names of Substances
- Proteins MeSH
The application of continuous flow-extractive desorption electrospray ionization (CF-EDESI), an ambient ionization source demonstrated previously for use with intact protein analysis, is expanded here for the coupling of reversed phase protein separations to mass spectrometry. This configuration allows the introduction of charging additives to enhance detection without affecting the chromatographic separation mechanism. Two demonstrations of the advantages of CF-EDESI are presented in this work. First, a proof-of- principle is presented to demonstrate the applicability of hyphenation of liquid chromatography (LC) to CF- EDESI. LC-CF-EDESI-MS has good sensitivity compared to LC-electrospray ionization (ESI)-mass spectrometry. Second, the supercharging mechanism investigated in CF-EDESI provides an insight into a highly debated supercharging process in ESI. The results indicate that the mechanism of protein charging seen in HPLC-CF-EDESI is different from supercharging phenomena in conventional ESI. The surface tension mechanism and binding mechanism may both contribute to protein supercharging in ESI.
References provided by Crossref.org
