CE–ESI‐MS for bottom‐up proteomics: Advances in separation, interfacing and applications
Abstract
With the development of more sensitive hyphenation strategies for capillary electrophoresis–electrospray‐mass spectrometry the technique has reemerged as technique with high separation power combined with high sensitivity in the analysis of peptides and protein digests. This review will discuss the newly developed hyphenation strategies for CE–ESI‐MS and their application in bottom‐up proteomics as well as the applications in the same time span, 2009 to present, using co‐axial sheathliquid. Subsequently all separate aspects in the development of a CE–ESI‐MS method for bottom‐up proteomics shall be discussed, highlighting certain applications and discussing pros and cons of the various choices. The separation of peptides in a capillary electrophoresis system is discussed including the great potential for modeling of this migration of peptides due to the simple electrophoretic separation process. Furthermore, the technical aspects of method development are discussed, namely; background electrolyte choice, coating of the separation capillary and chosen loading method. Finally, conclusions and an outlook on future developments in the field of bottom‐up proteomics by CE–ESI‐MS will be provided. © 2014 Wiley Periodicals, Inc. Mass Spec Rev 35:259–271, 2016.
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A potential limitation of the sheath-liquid interface is that high sheath-liquid flow dilutes the analyte and can cause sensitivity loss.
“A potential limitation of the sheath-liquid interface is that the high flow rate of the sheath-liquid dilutes the analyte, thereby causing a potential loss in sensitivity5,13.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [13]
tITP requires optimization of both electrolyte concentrations and loading volume for efficient stacking of target analytes.
“tITP requires an optimization of both electrolyte concentrations and loading volume to enable efficient stacking of the target analytes13,27,65,120–122.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [13]
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- Authors
- Heemskerk, A. A. M., Deelder, A. M., & Mayboroda, O. A.
- Affiliations
- Leiden University Medical Center (NL)
- Corresponding author
- Heemskerk, Anthonius A.M.
- ORCID
- Mayboroda, Oleg A.
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2014-05-23
- Volume
- 35
- Issue
- 2
- Pages
- 259-271
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W1575991501
- Cited by
- 61
- References
- 87
- Citations by year
- 2026: 1 · 2023: 2 · 2021: 6 · 2020: 4 · 2019: 7 · 2018: 9 · 2017: 11 · 2016: 11 · 2015: 6 · 2014: 3 · 2013: 1
- FWCI
- 1.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Mass Spectrometry Reviews (publishedVersion)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Keywords
- shotgun proteomics, peptide separation, supporting electrolyte, capillary coating
- MeSH terms
- Algorithms, Peptide Mapping, Specimen Handling, Systems Integration, Electrophoresis, Capillary, Proteome, Spectrometry, Mass, Electrospray Ionization, Proteomics
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