Online Hydrophobic Interaction Chromatography–Mass Spectrometry for the Analysis of Intact Monoclonal Antibodies
Open accessAbstract
Therapeutic monoclonal antibodies (mAbs) are an important class of drugs for a wide spectrum of human diseases. Liquid chromatography (LC) coupled to mass spectrometry (MS) is one of the techniques in the forefront for comprehensive characterization of analytical attributes of mAbs. Among various protein chromatography modes, hydrophobic interaction chromatography (HIC) is a popular offline nondenaturing separation technique utilized to purify and analyze mAbs, typically with the use of non-MS-compatible mobile phases. Herein we demonstrate for the first time, the application of direct HIC-MS and HIC-tandem MS (MS/MS) with electron capture dissociation (ECD) for analyzing intact mAbs on quadrupole-time-of-flight (Q-TOF) and Fourier transform ion cyclotron resonance (FTICR) mass spectrometers, respectively. Our method allows for rapid determination of relative hydrophobicity, intact masses, and glycosylation profiles of mAbs as well as sequence and structural characterization of the complementarity-determining regions in an online configuration.
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Chen et al. demonstrated online HIC-MS for determination of relative hydrophobicity, intact masses, and glycosylations of monoclonal antibodies and for gaining sequence and structural information using MS/MS.
“Chen et al. demonstrated online HIC-MS analysis for determination of the relative hydrophobicity, intact masses, and glycosylations of monoclonal antibodies (mAb) as well as gaining sequence and structural information using MS/MS [81].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [81]
The advancement of top-down proteomics is stimulated by commercial growth of large molecule therapeutics such as monoclonal antibodies and antibody-drug-conjugates, because detailed high-throughput characterization and quality control methods are required.
“Undoubtedly, the advancement of top-down proteomics is stimulated by the commercial growth of large molecule therapeutics such as monoclonal antibodies and antibody-drug-conjugates as detailed and high-throughput methods for their characterization and quality control are required [81,159,160].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [81]
Analysis of antibodies by top-down can quickly determine modification state, drug conjugate ratio, quality control screening, and more.
“For example, analysis of antibodies by top-down can quickly determine the modification state [81], drug conjugate ratio [161], quality control screening [162], and more [163,164].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [81]
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Therapeutic Proteins and Hyphenated Methods for Characterization
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Self-citation
- Authors
- Chen, B., Lin, Z., Alpert, A. J., Fu, C., Zhang, Q., Pritts, W. A., & Ge, Y.
- Affiliations
- University of Wisconsin–Madison (US)
- PolyLC Inc., Columbia, Maryland 21045, United States
- AbbVie (United States) (US)
- Corresponding author
- Ge, Ying
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-05-30
- Volume
- 90
- Issue
- 12
- Pages
- 7135-7138
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC6109971
- OpenAlex
- W2807004475
- Cited by
- 82
- References
- 26
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 11 · 2023: 8 · 2022: 13 · 2021: 7 · 2020: 19 · 2019: 11
- FWCI
- 3.99
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL096971, R01HL109810)
- AbbVie
- National Institute of General Medical Sciences (GM117058)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
- Keywords
- monoclonal antibodies, hydrophobic interaction chromatography, glycosylation profiling, hypervariable region, relative hydrophobicity, therapeutic proteins, tandem mass spectrometry, electron capture dissociation, protein structural characterization
- MeSH terms
- Antibodies, Monoclonal, Chromatography, Liquid, Humans, Mass Spectrometry, Hydrophobic and Hydrophilic Interactions
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