Cited by 110Advanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and ApplicationsProtein purification and stability

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Online Hydrophobic Interaction Chromatography–Mass Spectrometry for Top-Down Proteomics

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Chen, Bifan, Peng, Ying, Valeja, Santosh G., Xiu, Lichen, Alpert, Andrew J., Ge, Ying·2016·Analytical Chemistry

DOI 10.1021/acs.analchem.5b04285PMC PMC4947469

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Abstract

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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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
ORCID: Chen, Bifan
Xiu, Lichen
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
DOI: 10.1021/acs.analchem.5b04285
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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Online Hydrophobic Interaction Chromatography–Mass Spectrometry for Top-Down Proteomics

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