ArticleAnalytical chemistry2025
Nanoflow Size Exclusion Chromatography-Native Mass Spectrometry of Intact Proteoforms and Protein Complexes.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Polarity- and Sequence-Dependent Ionization of Therapeutic Antibody-siRNA Conjugates: Enabling Intact Multi-attribute Method for Comprehensive Characterization and Identity Release Assay.Analytical chemistry · 2026Article
- Development and Validation of SEC-UV/HRMS Procedure for Simultaneous Determination of BSA and Its Association Products.Molecules (Basel, Switzerland) · 2026Article
- On the Utility of Infrared Photoactivation for Native Top-Down and Complex-Down Orbitrap Mass Spectrometry of Soluble Proteoform Complexes.Journal of the American Society for Mass Spectrometry · 2026Article
- Multiple Heart-Cut Ion-Exchange Chromatography-Reversed-Phase Liquid Chromatography Platform for Online Desalting and Fractionation of Monoclonal Antibody Charge Variants.Journal of separation science · 2026Article
- Developments in Ion Exchange Chromatography-Mass Spectrometry for the Characterization of Intact Proteins and Proteoforms.Journal of separation science · 2025Review
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Authors and funding
7 authors.
Funding
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Abstract
Native size-exclusion chromatography (SEC) coupled with native mass spectrometry (nMS) enables the characterization of proteins and protein complexes by combining liquid-phase separation (SEC) and mass measurement (nMS). This approach allows for an increase in the throughput of nMS experiments, reduces the bias that may be present due to the co-ionization of oligomers, and facilitates online sample buffer exchange. Conventional SEC-nMS uses volatile buffers and relatively wide-diameter columns (e.g., ≥1 mm), with flow rates in the tens of μL/min. To ionize sample components under this flow regime, relatively harsh electrospray ionization (ESI) desolvation conditions are needed, potentially resulting in protein dissociation/denaturation. Additionally, relatively large amounts of samples are required (several μgs). Herein, we describe the development of a nanoflow SEC-nMS method using 200 μm I.D. columns, operated at 500 nL min
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