ArticleJournal of proteome research2025
Gel-Based Sample Fractionation with SP3-Purification for Top-Down Proteomics.
Article in Journal of proteome research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- A Novel Protein Recovery Method via Gel Separation and Silica Columns Capable of Rapid Antigen Purification and Deep Proteomic Identification.Molecules (Basel, Switzerland) · 2026Article
- PEPPI-SP3: A Gel-Based High-Resolution Sample Preparation Workflow for In-Depth Top-Down Analysis of Intact Proteoforms by Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Comparative Analysis of Proteoform Clean-Up Methods for In-Depth Top-Down Proteomics.Proteomics · 2025Article
- Sample preparation and cleanup methods for clinical top-down proteomics.Expert review of proteomics · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Precise prefractionation of proteome samples is a potent method for realizing in-depth analysis in top-down proteomics. PEPPI-MS (Passively Eluting Proteins from Polyacrylamide gels as Intact species for MS), a gel-based sample fractionation method, enables high-resolution proteome fractionation based on molecular weight by highly efficient extraction of proteins from polyacrylamide gels after SDS-PAGE separation. Thereafter it is essential to effectively remove contaminants such as CBB and SDS from the PEPPI fraction prior to mass spectrometry. In this study, we developed a complete, robust, and simple sample preparation workflow named PEPPI-SP3 for top-down proteomics by combining PEPPI-MS with the magnetic bead-based protein purification approach used in SP3 (single-pot, solid-phase-enhanced sample preparation), now one of the standard sample preparation methods in bottom-up proteomics. In PEPPI-SP3, proteins extracted from the gel are collected on the surface of SP3 beads, washed with organic solvents, and recovered intact with 100 mM ammonium bicarbonate containing 0.05% (w/v) SDS. The recovered proteins are subjected to mass spectrometry after additional purification using an anion-exchange StageTip. Performance validation using human cell lysates showed a significant improvement in low-molecular-weight protein recovery with a lower coefficient of variation compared to conventional PEPPI workflows using organic solvent precipitation or ultrafiltration.
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Registered trials
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