ArticleThe Analyst2020
Online capillary electrophoresis - mass spectrometry analysis of histatin-5 and its degradation products.
Article in The Analyst, 2020. 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
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Optimizing Histatin 5: Effects of K13 and K17 Substitutions on Proteolytic Stability and Antifungal Activity.Computational and structural biotechnology journal · 2026Article
- A Comprehensive Review on Capillary Electrophoresis-Mass Spectrometry in Advancing Biomolecular Research.Electrophoresis · 2025Review
- Rapid identification of antibody impurities in size-based electrophoresis via CZE-MS generated spectral library.Scientific reports · 2024Article
- Recent advances (2019-2021) of capillary electrophoresis-mass spectrometry for multilevel proteomics.Mass spectrometry reviews · 2023Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Histatin-5 (Hst-5) is a human salivary peptide with antibacterial and antifungal activities. Thorough characterization and reliable quantification of Hst-5 and its degradation products are essential for understanding the Hst-5 degradation pathway. Due to the highly basic and strong cationic nature of the Hst-5 peptide, the quantitative analysis of Hst-5 and its degradation forms by online mass spectrometry remains challenging. Here, we adopt a recently developed electrokinetically pumped sheath liquid capillary electrophoresis - mass spectrometry (CE-MS) coupling technology, and successfully apply it for the analysis of Hst-5 and its degradation products. Our CE-MS method is demonstrated to be robust and quantitative. This novel analytical platform is reproducible and free of sample carryover. The efficacy of this method is demonstrated with a kinetic study of Hst-5 degradation by Sap9, a secreted aspartic peptidase. Our work demonstrates the potential of online CE-MS as a powerful approach for characterizing highly basic peptides.
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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.