ArticleAnalytical chemistry2025
Top-Down Proteomic Analysis of Limited Samples Using Porous Layer Open Tubular Columns and High-Field Asymmetric Ion Mobility Spectrometry Coupled to Mass Spectrometry.
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 3 papers.
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Who cites it
3 citing papers in PubMed.
- Top-Down versus Bottom-Up Proteomics in Highly Sensitive LC-MS-Based Profiling of Limited Samples.Analytical chemistry · 2026Article
- Capturing Cardiomyocyte Cell-to-Cell Heterogeneity via Shotgun Single Cell Top-Down Proteomics.bioRxiv : the preprint server for biology · 2026Article
- Intact Proteoform Analysis by Capillary Electrophoresis-Mass Spectrometry. Are We There Yet?Angewandte Chemie (International ed. in English) · 2026Article
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6 authors.
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Abstract
Despite significant recent progress in the field of mass spectrometry (MS)-based top-down proteomics (TDP), the analysis of limited samples is still a major challenge. Here, we explored the potential of ultralow flow (ULF) liquid chromatography (LC) porous layer open tubular (PLOT) columns interfaced with MS via high-field asymmetric waveform ion mobility spectrometry (FAIMS) to enable high-sensitivity TDP analysis of small populations of mammalian cells. The developed robust and easy-to-use platform delivered high reproducibility of retention times (RSD < 0.4%) and high separation performance for intact proteins (∼14-s peak full width at half-maximum and peak capacity of >125 for a 60 min effective gradient). The FAIMS-based experiments resulted in a ∼2-fold increase in identifications compared to the control experiments for ∼200 HeLa cell aliquots, i.e., 819 vs 454 proteins and 2645 vs 1305 proteoforms, respectively. The pilot ULF LC-MS analysis of six HeLa cells yielded 29 ± 3 proteins and 38 ± 2 proteoforms, on average, and a total of 44 proteins and 68 proteoforms. Data revealed a high degree of acetylation, methylation, phosphorylation, glycosylation, lactylation, and other relevant post-translational modifications. Notably, the presented protein identification results for limited samples are comparable to those of recent large-scale TDP studies of bulk samples, demonstrating the potential to enable informative single-cell TDP profiling.
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