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Review
. 2019 Nov;38(6):445-460.
doi: 10.1002/mas.21599. Epub 2019 Aug 12.

Recent trends of capillary electrophoresis-mass spectrometry in proteomics research

Affiliations
Review

Recent trends of capillary electrophoresis-mass spectrometry in proteomics research

Fabio P Gomes et al. Mass Spectrom Rev. 2019 Nov.

Abstract

Progress in proteomics research has led to a demand for powerful analytical tools with high separation efficiency and sensitivity for confident identification and quantification of proteins, posttranslational modifications, and protein complexes expressed in cells and tissues. This demand has significantly increased interest in capillary electrophoresis-mass spectrometry (CE-MS) in the past few years. This review provides highlights of recent advances in CE-MS for proteomics research, including a short introduction to top-down mass spectrometry and native mass spectrometry (native MS), as well as a detailed overview of CE methods. Both the potential and limitations of these methods for the analysis of proteins and peptides in synthetic and biological samples and the challenges of CE methods are discussed, along with perspectives about the future direction of CE-MS. @ 2019 Wiley Periodicals, Inc. Mass Spec Rev 00:1-16, 2019.

Keywords: capillary electrophoresis-mass spectrometry; electrospray ionization; native mass spectrometry; proteomics; top-down mass spectrometry.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1.
Figure 1.
Schematic of a TDMS workflow. Reproduced from reference , with permission from The Royal Society of Chemistry.
Figure 2.
Figure 2.
Schematic of the information obtained from native MS experiment. Reprinted from reference , with permission.
Figure 3.
Figure 3.
Schematic representations of (A) porous ESI tip sheathless interface and (B) electrokinetically pumped sheath-flow nanospray. Reprinted from references and , respectively, with permission,.
Figure 3.
Figure 3.
Schematic representations of (A) porous ESI tip sheathless interface and (B) electrokinetically pumped sheath-flow nanospray. Reprinted from references and , respectively, with permission,.
Figure 4. and Figure 5.
Figure 4. and Figure 5.
Base peak electropherogram of a CZE separation for top-down analysis in Escherichia coli proteome. Reprinted from reference , with permission. Intensity of the proteins from the CZE-MS method with different BGEs and concentrations. Reprinted from reference , with permission.
Figure 6.
Figure 6.
ESI mass spectra of myoglobin in aqueous solution at pH 7. The salt concentrations (ammonium acetate and ammonium bicarbonate) increase from A to C and from D to F. Reprinted from reference , with permission.
Figure 7.
Figure 7.
Elution profiles of (1) cytochrome c, (2) lysozyme, (3) ribonuclease A, and (4) chymotrypsinogen A on uncoated and LPA coated capillaries at the same electrophoretic conditions. Reprinted from reference , with permission.

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