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Online Hydrophobic Interaction Chromatography–Mass Spectrometry for Top-Down Proteomics
Open accessAbstract
Recent progress in top-down proteomics has led to a demand for mass spectrometry (MS)-compatible chromatography techniques to separate intact proteins using volatile mobile phases. Conventional hydrophobic interaction chromatography (HIC) provides high-resolution separation of proteins under nondenaturing conditions but requires high concentrations of nonvolatile salts. Herein, we introduce a series of more-hydrophobic HIC materials that can retain proteins using MS-compatible concentrations of ammonium acetate. The new HIC materials appear to function as a hybrid form of conventional HIC and reverse phase chromatography. The function of the salt seems to be preserving protein structure rather than promoting retention. Online HIC-MS is feasible for both qualitative and quantitative analysis. This is demonstrated with standard proteins and a complex cell lysate. The mass spectra of proteins from the online HIC-MS exhibit low charge-state distributions, consistent with those commonly observed in native MS. Furthermore, HIC-MS can chromatographically separate proteoforms differing by minor modifications. Hence, this new HIC-MS combination is promising for top-down proteomics.
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“Hydrophobic interaction chromatography (HIC)-MS shows great promise for characterizing intact protein directly coupled to top-down MS [80].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [80]
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“Recently, high-throughput native separation techniques including GELFrEE,36 HIC,39,40 SEC,112 capillary zone electrophoresis (CZE),112 and IEX38 have efficiently aided in the analysis of heterogeneous protein mixtures.”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [39]
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Self-citation
Metadata
- Authors
- Chen, B., Peng, Y., Valeja, S. G., Xiu, L., Alpert, A. J., & Ge, Y.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Alpert, Andrew J.
- Ge, Ying
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-01-14
- Volume
- 88
- Issue
- 3
- Pages
- 1885-1891
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC4947469
- OpenAlex
- W2229695971
- Cited by
- 110
- References
- 49
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 7 · 2023: 6 · 2022: 14 · 2021: 7 · 2020: 13 · 2019: 13 · 2018: 10 · 2017: 16 · 2016: 9
- FWCI
- 7.97
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH Office of the Director (S10OD01847)
- National Heart, Lung, and Blood Institute (R01HL096971, R01HL109810)
- National Institute of General Medical Sciences (R01GM11705)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- hydrophobic interaction chromatography, top-down proteomics, protein retention, reverse-phase chromatography, proteoforms, protein modification, native mass spectrometry, protein structure preservation, cell lysate analysis
- MeSH terms
- Animals, Cattle, Chickens, Chromatography, Chymotrypsinogen, Horses, Aprotinin, Lactoglobulins, Muramidase, Ribonuclease, Pancreatic, Mass Spectrometry, Trypsinogen, Internet, Proteomics, Hydrophobic and Hydrophilic Interactions
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