Optimizing capillary electrophoresis for top‐down proteomics of 30–80 kDa proteins
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The direct analysis of intact proteins via MS offers compelling advantages in comparison to alternative methods due to the direct and unambiguous identification and characterization of protein sequences it provides. The inability to efficiently analyze proteins in the “middle mass range,” defined here as proteins from 30 to 80 kDa, in a robust fashion has limited the adoption of these “top‐down” methods. Largely, a result of poor liquid chromatographic performance, the limitations in this mass range may be addressed by alternative separations that replace chromatography. Herein, the short migration times of CZE‐ESI‐MS/MS have been extended to size‐sorted whole proteins in complex mixtures from Pseudomonas aeruginosa PA01 . An electrokinetically pumped nanospray interface, a coated capillary, and a stacking method for on‐column sample concentration were developed to achieve high‐loading capacity and separation resolution. We achieved full width at half maximum of 8–16 s for model proteins up to 29 kDa and identified 30 proteins in the mass range of 30–80 kDa from P. aeruginosa PA01 whole cell lysate. These results suggest that CZE‐ESI‐MS/MS is capable of identifying proteins in the middle mass range in top‐down proteomics.
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A PA coated capillary separated intact proteins with molecular masses from 30 to 80 kDa.
“The Kelleher group demonstrated the use of a PA coated capillary for the separation of intact proteins with molecular masses ranging from 30 to 80 kDa.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [110]
Thirty proteins were identified from P. aeruginosa PA01 whole cell lysate using a PA coated capillary.
“In this study, 30 proteins were identified from P. aeruginosa PA01 whole cell lysate110.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [110]
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Self-citation
- Authors
- Li, Y., Compton, P. D., Tran, J. C., Ntai, I., & Kelleher, N. L.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Kelleher, Neil L.
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2014-04-10
- Volume
- 14
- Issue
- 10
- Pages
- 1158-1164
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- PMC
- PMC4034378
- OpenAlex
- W2076807510
- Cited by
- 95
- References
- 24
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 5 · 2023: 3 · 2022: 5 · 2021: 6 · 2020: 3 · 2019: 12 · 2018: 8 · 2017: 15 · 2016: 12 · 2015: 12 · 2014: 6
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- PROTEOMICS (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- IUScholarWorks (Indiana University) (submittedVersion, cc-by)
- Funders
- National Institute of General Medical Sciences
- National Institute of Drug Abuse of the National Institutes of Health (R01 GM067193, DA018310)
- National Science Foundation (ABI-1062432)
- Chicago Biomedical Consortium
- Searle Funds at The Chicago Community Trust
- National Center for Genome Analysis Support
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- top-down proteomics, capillary zone electrophoresis, coated capillaries, sample concentration, Pseudomonas aeruginosa PAO1, whole cell lysate
- MeSH terms
- Amino Acid Sequence, Molecular Sequence Data, Proteins, Reproducibility of Results, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization, Proteomics, Tandem Mass Spectrometry
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