CE‐MS for the analysis of intact proteins 2010–2012
Abstract
Since its introduction in 1987, CE‐MS has become an increasingly important technique for the analysis of biomolecules. Since our previous update on CE‐MS methods within the field of intact protein analysis (Electrophoresis 2011, 32, 66–82), a variety of interesting methodological improvements and applications have been reported in literature. Therefore, this article presents an overview of the development and application of CE‐MS for intact protein analysis as published between June 2010 and June 2012. The article is divided in sections that treat CE coupled to MS through ESI, MALDI, and ICP ionization, respectively. In the section about CE‐ESI‐MS, technological developments with respect to CE‐MS interfacing, prevention of protein adsorption, and chip‐based CE‐MS are treated in more detail. Novel interfacing strategies and the development of improved capillary coating strategies appeared to be the major developments. Furthermore, in all sections, the applicability of CE‐MS for intact protein analysis is demonstrated by representative examples, including important developments in the fields of biopharmaceutical characterization and the analysis of proteins in biological samples. Finally, some general conclusions and future perspectives are given.
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Top-down analysis can provide unique structural insights into proteins through precise molecular weight measurements, identification of multiple PTMs, and in-depth proteoform characterization.
“Top-down analysis can provide unique insights into a protein’s structure by providing precise molecular weight measurements, the identification of multiple PTMs5,16,28 and in-depth proteoform characterization (different forms of a single protein generated from a gene)32.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [28]
CZE is particularly attractive for protein analysis because proteins have small diffusion coefficients.
“This is particularly attractive for protein analysis because they have small diffusion coefficients28,29.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [28]
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References 71 · Cited by 96
- Authors
- Haselberg, R., de Jong, G. J., & Somsen, G. W.
- Affiliations
- Utrecht University (NL)
- Biomolecular Analysis Utrecht University CG Utrecht The Netherlands
- Corresponding author
- Haselberg, Rob
- Venue
- ELECTROPHORESIS
- Publisher
- Wiley
- Published
- 2012-12-03
- Volume
- 34
- Issue
- 1
- Pages
- 99-112
- ISSN
- 0173-0835 (ISSN-L)
- 1522-2683
- OpenAlex
- W1529015150
- Cited by
- 96
- References
- 71
- Citations by year
- 2024: 1 · 2023: 2 · 2022: 3 · 2021: 7 · 2020: 2 · 2019: 5 · 2018: 7 · 2017: 10 · 2016: 15 · 2015: 15 · 2014: 12 · 2013: 15 · 2012: 1
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Electrophoresis (publishedVersion)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- capillary electrophoresis-mass spectrometry, top-down proteomics, protein adsorption prevention, capillary coating, biopharmaceutical characterization
- MeSH terms
- Adsorption, Humans, Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization, Lab-On-A-Chip Devices
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