ArticleAnalytical sciences : the international journal of the Japan Society for Analytical Chemistry2020
Direct Detection of Lysozyme in Viscous Raw Hen Egg White Binding to Sodium Dodecyl Sulfonate by Reactive Wooden-tip Electrospray Ionization Mass Spectrometry.
Article in Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, 2020. 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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3 citing papers in PubMed, 8 citations in OpenAlex.
- Direct mass spectrometry analysis of biological tissue for diagnosis of thyroid cancer using wooden-tip electrospray ionization.Frontiers in chemistry · 2023Article
- Pre-cleaned bare wooden toothpicks for the determination of drugs in oral fluid by mass spectrometry.Analytical and bioanalytical chemistry · 2022Article
- Wooden-Tip Electrospray Mass Spectrometry Characterization of Human Hemoglobin in Whole Blood Sample for Thalassemia Screening: A Pilot Study.Molecules (Basel, Switzerland) · 2022Article
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6 authors at 2 institutions in 1 country.
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Abstract
Direct characterization of native protein binding to ligands in raw biological samples is a challenging task, because the ligand solution might induce proteins to aggregation, flocculation and denaturation. In this work, we developed a reactive wooden-tip electrospray ionization mass spectrometry (ESI-MS) for formation and characterization of protein-ligand complexes upon rapid mixing in electrospray droplets. Raw viscous hen egg white (HEW) was directly loaded onto a wooden tip to induce spray ionization, and sodium dodecyl sulfonate (SDS) solution was directly loaded into the HEW spray by a pipette tip, and thus lysozyme-DS complexes were then formed in the electrospray droplets and were detected subsequently by mass spectrometry. The new approach was successfully applied to investigate interaction of SDS and native lysozyme in electrospray droplets of standard solution and raw egg white. Our results showed that wooden-tip ESI-MS is a promising method to form and characterize protein-ligand complexes.
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