ArticleElectrophoresis2024
Protein analysis using capillary electrophoresis coupled to mass spectrometry through vibrating sharp-edge spray ionization.
Article in Electrophoresis, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The trial behind it
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Native CZE-MS analysis of antibodies and hemoglobin using protein-adapted CZE and ESI conditions for detailed proteoform characterization.Analytical and bioanalytical chemistry · 2026Article
- Research advances in capillary electrophoresis coating technology for protein analysis.Analytical and bioanalytical chemistry · 2026Review
- Capillary Electrophoresis Mass Spectrometry Interfacing via Multifunctional Vibrating Sharp Edge Ionization Spray for the Simultaneous Delivery of an Auxiliary Flow, Analyte Mixing, and Fluid Nebulization.Analytical chemistry · 2026Article
- Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025Review
- Does Native Capillary Zone Electrophoresis-Mass Spectrometry Maintain the Structural Topology of Protein Complexes?Analytical chemistry · 2025Article
- Evaluation of a cIEF Fractionation Workflow for Offline MS Analysis of Charge Variants of the Monoclonal Antibody Matuzumab.Electrophoresis · 2025Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Capillary electrophoresis (CE) interfaced to mass spectrometry (MS) with electrospray ionization typically incorporates acidic additives or organic solvents to assist in ionization. Vibrating sharp-edge spray ionization (VSSI) is a voltage-free method to interface CE and MS that does not require these additives, making it appealing for protein analyses. CE-VSSI nanoflow sheath separations are performed with low ionic strength aqueous solutions in the sheath to reduce suppression. Serine is also included in the sheath to reduce analyte adduction. Proteins are detected in the 2.5-10 µM range, corresponding to an injected mass range of 0.1-1.2 ng. The anionic proteins β-lactoglobulin and transferrin are resolved using an unmodified fused silica capillary because they do not exhibit nonspecific surface adsorption. Conversely, separations of cationic proteins cytochrome c, ribonuclease A, and α-chymotrypsinogen A in an unmodified capillary require acidic background electrolytes to overcome adsorption. Alternatively, a semipermanent coating comprised self-assembled lipids overcomes surface adsorption at a neutral pH. Separations with zwitterionic and hybrid cationic coatings are complete within 15 or 6 min, respectively. The dimeric form of triosephosphate isomerase was observed at a 60 µM, corresponding to a mass of 19 ng, by dropping the temperature of the MS inlet.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.