Analysis of Proteins, Protein Complexes, and Organellar Proteomes Using Sheathless Capillary Zone Electrophoresis - Native Mass Spectrometry
Open accessAbstract
Native mass spectrometry (MS) is a rapidly advancing field in the analysis of proteins, protein complexes, and macromolecular species of various types. The majority of native MS experiments reported to-date has been conducted using direct infusion of purified analytes into a mass spectrometer. In this study, capillary zone electrophoresis (CZE) was coupled online to Orbitrap mass spectrometers using a commercial sheathless interface to enable high-performance separation, identification, and structural characterization of limited amounts of purified proteins and protein complexes, the latter with preserved non-covalent associations under native conditions. The performance of both bare-fused silica and polyacrylamide-coated capillaries was assessed using mixtures of protein standards known to form non-covalent protein-protein and protein-ligand complexes. High-efficiency separation of native complexes is demonstrated using both capillary types, while the polyacrylamide neutral-coated capillary showed better reproducibility and higher efficiency for more complex samples. The platform was then evaluated for the determination of monoclonal antibody aggregation and for analysis of proteomes of limited complexity using a ribosomal isolate from E. coli. Native CZE-MS, using accurate single stage and tandem-MS measurements, enabled identification of proteoforms and non-covalent complexes at femtomole levels. This study demonstrates that native CZE-MS can serve as an orthogonal and complementary technique to conventional native MS methodologies with the advantages of low sample consumption, minimal sample processing and losses, and high throughput and sensitivity. This study presents a novel platform for analysis of ribosomes and other macromolecular complexes and organelles, with the potential for discovery of novel structural features defining cellular phenotypes (e.g., specialized ribosomes). Graphical Abstract ᅟ.
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Belov and co-workers successfully applied an etched porous-tip sheathless interface to analyze complex-forming protein standards, a monoclonal antibody, and an Escherichia coli ribosomal proteome under native conditions.
“In a recent paper, Belov and co-workers reported a successful application of an etched porous-tip sheathless interface for analysis of complex-forming protein standards, a monoclonal antibody, and a ribosomal proteome of the Escherichia coli in native conditions35.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
Native MS provides a proteomics tool that enables identification and characterization of biomolecular structures and advances understanding of biological pathways at the molecular level.
“Native MS provides a proteomics tool that enables identification and characterization of these biomolecular structures and advances the understanding of their biological pathways at the molecular level19,20,35.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
Most TDMS studies are performed under denaturing conditions, which disrupts biologically relevant non-covalent interactions such as protein-protein and protein-ligand complexes.
“Most TDMS studies are carried out under denaturing conditions, leading to the disruption of the biologically relevant non-covalent interactions, such as protein-protein and protein-ligand complexes35.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
The ultra-low flow rates of this interface enabled higher sensitivity than sheath-liquid designs.
“The ultra-low flow rates enabled higher sensitivity from this interface than from sheath-liquid designs.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
Native MS provides information about ligand binding, dynamics, subunit stoichiometry, stability, topology, and assembly structural properties.
“Native MS provides information about ligand binding, dynamics, stoichiometry of individual subunits, stability, topology, and assembly structural properties35.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
This interface enabled protein characterization without dilution before nano-ESI flow rates of 10-20 nL/min.
“This interface enabled characterization of proteins without dilution prior to nano-ESI flow rates (10–20 nL/min).”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
Bare fused silica capillaries gave marginal separation efficiency for intact proteins and protein complexes because of protein adsorption, whereas neutral coated capillaries gave high separation efficiency by preventing adsorption.
“The bare fused silica capillary produced a marginal separation efficiency for intact proteins and protein complexes as a result of protein adsorption to the capillary wall, whereas the neutral coated capillary generated high separation efficiency by preventing protein adsorption35.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [35]
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Self-citationShen, X., Kou, Q., Guo, R., Yang, Z., Chen, D., Liu, X., Hong, H., & Sun, L. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02725 · Cited by 78 · see citing works
- Authors
- Belov, A. M., Viner, R., Santos, M. R., Horn, D. M., Bern, M., Karger, B. L., & Ivanov, A. R.
- Affiliations
- Northeastern University (US)
- Thermo Fisher Scientific (United States) (US)
- SCIEX, 92821, Brea, CA, USA
- Protein Metrics (United States) (US)
- Venue
- Journal of the American Society for Mass Spectrometry
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-09-05
- Volume
- 28
- Issue
- 12
- Pages
- 2614-2634
- ISSN
- 1044-0305 (ISSN-L)
- PMC
- PMC5709234
- OpenAlex
- W2752396658
- Cited by
- 97
- References
- 88
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 5 · 2023: 4 · 2022: 17 · 2021: 17 · 2020: 13 · 2019: 13 · 2018: 13 · 2017: 3 · 2015: 1
- FWCI
- 5.66
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of the American Society for Mass Spectrometry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1R01GM120272)
- American Society for Mass Spectrometry
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Keywords
- native mass spectrometry, capillary zone electrophoresis, protein complexes, protein-ligand complex, monoclonal antibody aggregation, Escherichia coli ribosome, polyacrylamide-coated capillary, proteoforms, organelle proteome, tandem mass spectrometry
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Cattle, Escherichia coli, Proteins, Rabbits, Saccharomyces cerevisiae, Mass Spectrometry, Electrophoresis, Capillary, Proteome, Saccharomyces cerevisiae Proteins, Escherichia coli Proteins, Sus scrofa, Proteomics, Workflow
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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