Capillary HILIC-MS: A New Tool for Sensitive Top-Down Proteomics
Open accessAbstract
Recent progress in top-down proteomics has driven the demand for chromatographic methods compatible with mass spectrometry (MS) that can separate intact proteins. Hydrophilic interaction liquid chromatography (HILIC) has recently shown good potential for the characterization of glycoforms of intact proteins. In the present study, we demonstrate that HILIC can separate a wide range of proteins exhibiting orthogonal selectivity with respect to reversed-phase LC (RPLC). However, the application of HILIC to the analysis of low abundance proteins (e.g., in proteomics analysis) is hampered by low volume loadability, hindering down-scaling of the method to column diameters below 2.1 mm. Moreover, HILIC-MS sensitivity is decreased due to ion suppression from the trifluoroacetic acid (TFA) often used as the ion-pair agent to improve the selectivity and efficiency in the analysis of glycoproteins. Here, we introduce a capillary-based HILIC-MS method that overcomes these problems. Our method uses RPLC trap-columns to load and inject the sample, circumventing issues of protein solubility and volume loadability in capillary columns (200 μm ID). The low flow rates and use of a dopant gas in the electrospray interface improve protein-ionization efficiencies and reduce suppression by TFA. Overall, this allows the separation and detection of small protein quantities (down to 5 ng injected on column) as indicated by the analysis of a mixture of model proteins. The potential of the new capillary HILIC-MS is demonstrated by the analysis of a complex cell lysate.
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Gargano et al. developed online capillary HILIC for top-down proteomics.
“More recently, Gargano et al. developed online capillary HILIC for top-down proteomics [76].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [76]
HILIC proteome coverage was limited and significant work remains before its full potential for top-down proteomics is recognized.
“However, the proteome coverage was limited and significant work will still be needed before the full potential of HILIC for top-down proteomics is recognized.”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [76]
They used a C4 trap column for loading and doped propionic acid in the electrospray interface to overcome signal suppression of trifluoroacetic acid in the mobile phase.
“Notably, they utilized a C4 trap column for loading (bypassing the traditional use of high organic solvent for sample composition) and doped propionic acid in the electrospray interface to overcome the signal suppression of trifluoroacetic acid in the mobile phase [76].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [76]
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- Authors
- Gargano, A. F. G., Roca, L. S., Fellers, R. T., Bocxe, M., Domínguez-Vega, E., & Somsen, G. W.
- Affiliations
- Vrije Universiteit Amsterdam (NL)
- Centre for Analytical Science Amsterdam , Science Park 904 , ,
- Northwestern University (US)
- Vrije Universiteit Amsterdam , , de Boelelaan 1083 , ,
- Corresponding author
- Gargano, Andrea F.G.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-05-03
- Volume
- 90
- Issue
- 11
- Pages
- 6601-6609
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC5990932
- OpenAlex
- W2801628150
- Cited by
- 52
- References
- 42
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 6 · 2023: 7 · 2022: 5 · 2021: 8 · 2020: 10 · 2019: 6 · 2018: 4
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Analytical Chemistry (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UvA-DARE (University of Amsterdam) (publishedVersion, cc-by-nc-nd)
- Leiden Repository (Leiden University) (submittedVersion, cc-by-nc-nd)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- VU Research Portal (submittedVersion, other-oa)
- Leiden Repository (Leiden University) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (722.015.009)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Analytical Chemistry and Chromatography
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- hydrophilic interaction liquid chromatography, top-down proteomics, intact protein separation, low-abundance proteins, ion suppression, trifluoroacetic acid, electrospray ionization, glycoproteins, cell lysate analysis
- MeSH terms
- Algorithms, Chromatography, Liquid, Proteins, Mass Spectrometry, Trifluoroacetic Acid, Proteomics, Hydrophobic and Hydrophilic Interactions
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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