Capillary electrophoresis applied to proteomic analysis

Fonslow, Bryan R.; Yates III, John R.

doi:10.1002/jssc.200800592

Cited by 92Microfluidic and Capillary Electrophoresis ApplicationsAdvanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and Applications

Capillary electrophoresis applied to proteomic analysis

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Fonslow, Bryan R., Yates III, John R.·2009·Journal of Separation Science

DOI 10.1002/jssc.200800592PMC PMC3509210

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Abstract

In the postgenomic era, proteomics has become a dominant field for identifying and quantifying the complex protein machinery of the cell. The expression levels, posttranslational modifications, and specific interactions of proteins control the biology of such processes as development, differentiation, and signal transduction. Studies of the proteins involved in these processes often lead to a better understanding of biology and of human disease. Powerful separation techniques and sensitive detection methods enable researchers to untangle these complicated networks of processes. CE coupled with either MS or LIF are two of the techniques that make this possible. This review will cover proven CE‐based methods for proteomics on the cell and tissue level and their application in biological and clinical studies, relevant new developments in enabling technology such as microfluidic CE‐MS demonstrated on model systems, and comment on the future of CE in proteomics.

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Confident identification and quantification of proteins, PTMs, and peptides in biological samples depends on rigorous peptide separation before mass spectrometry.
“Confident identification and quantification of proteins, posttranslational modifications (PTMs), and peptides in biological samples rely on rigorous separation of peptides prior to introduction into the mass spectrometer1,5,6.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [5]
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 [5]
The main challenge of the sheathless configuration is maintaining CE flow while generating a closed electrical circuit between the CE separation and the ESI source.
“In this configuration, the main challenge is maintaining CE flow while generating a closed electrical circuit between the CE separation and the ESI source5.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [5]
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 [5]
The sheathless interface can significantly enhance signal-to-noise because analyte dilution and background noise are decreased when the BGE is the only liquid.
“In contrast, the sheathless interface can significantly enhance signal/noise due to decreased analyte dilution and background noise, as the BGE is the only liquid in the system5,54.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [5]

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Heller (2001) · doi:10.1002/1522-2683(200102)22:4

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[98]Mohan D Lee CS Electrophoresis 2002 23 3160 3167 12298088
[110]Kelleher NL Analytical chemistry 2004 76 197A 203A 15190879

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Authors: Fonslow, B. R., & Yates III, J. R.
Affiliations: Scripps Research Institute (US)
Venue: Journal of Separation Science
Publisher: Wiley
Published: 2009-04
Volume: 32
Issue: 8
Pages: 1175-1188
ISSN: 1615-9306 (ISSN-L)
1615-9314
DOI: 10.1002/jssc.200800592
PMC: PMC3509210
OpenAlex: W1980949566
Cited by: 92
References: 169
Citations by year: 2025: 1 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 2 · 2017: 6 · 2016: 4 · 2015: 7 · 2014: 4 · 2013: 11 · 2012: 10
FWCI: 8.83
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 8 d)
Locations: Journal of Separation Science (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (DK074798-02)
Topics: Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Keywords: capillary electrophoresis, proteomics, post-translational modification, protein-protein interaction, clinical proteomics, protein abundance
MeSH terms: Amino Acid Sequence, Humans, Molecular Sequence Data, Proteins, Sequence Alignment, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Electrophoresis, Capillary, Proteome, Spectrometry, Mass, Electrospray Ionization, Proteomics

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