ArticleJournal of proteome research2015
New mass-spectrometry-compatible degradable surfactant for tissue proteomics.
Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- SIMPLEX Enriches Hydrophobic and Lipidated Proteins in Membrane Proteomics Experiments.Proteomics · 2025Article
- Integrative proteomic and metabolomic elucidation of cardiomyopathy with in vivo and in vitro models and clinical samples.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Review
- Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry.ACS measurement science au · 2024Review
- Proteomics of the heart.Physiological reviews · 2024Review
- Enhanced Electrophoretic Depletion of Sodium Dodecyl Sulfate with Methanol for Membrane Proteome Analysis by Mass Spectrometry.Proteomes · 2024Article
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Immunopeptidomics in the Era of Single-Cell Proteomics.Biology · 2023Article
- Article
- Emergence of mass spectrometry detergents for membrane proteomics.Analytical and bioanalytical chemistry · 2023Review
- Label-free single cell proteomics utilizing ultrafast LC and MS instrumentation: A valuable complementary technique to multiplexing.Proteomics · 2023Review
- Synthesis, Self-Assembly Properties, and Degradation Characterization of a Nonionic Photocleavable Azo-Sulfide Surfactant Family.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Nonionic, Cleavable Surfactant for Top-Down Proteomics.Analytical chemistry · 2023Article
- Hanging drop sample preparation improves sensitivity of spatial proteomics.Lab on a chip · 2022Article
- Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021Review
- Surfactant-assisted one-pot sample preparation for label-free single-cell proteomics.Communications biology · 2021Article
- Differential Detergent Fractionation of Membrane Protein From Small Samples of Hepatocytes and Liver Tissue for Quantitative Proteomic Analysis of Drug Metabolizing Enzymes and Transporters.Journal of pharmaceutical sciences · 2021Article
- Divide-and-Conquer Matrisome Protein (DC-MaP) Strategy: An MS-Friendly Approach to Proteomic Matrisome Characterization.International journal of molecular sciences · 2020Article
- Top-down proteomics: challenges, innovations, and applications in basic and clinical research.Expert review of proteomics · 2020Article
- High-Throughput Proteomics Enabled by a Photocleavable Surfactant.Angewandte Chemie (International ed. in English) · 2020Article
- Sample Preparation by Easy Extraction and Digestion (SPEED) - A Universal, Rapid, and Detergent-free Protocol for Proteomics Based on Acid Extraction.Molecular & cellular proteomics : MCP · 2020Article
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Authors and funding
8 authors.
Funding
Abstract
Tissue proteomics is increasingly recognized for its role in biomarker discovery and disease mechanism investigation. However, protein solubility remains a significant challenge in mass spectrometry (MS)-based tissue proteomics. Conventional surfactants such as sodium dodecyl sulfate (SDS), the preferred surfactant for protein solubilization, are not compatible with MS. Herein, we have screened a library of surfactant-like compounds and discovered an MS-compatible degradable surfactant (MaSDeS) for tissue proteomics that solubilizes all categories of proteins with performance comparable to SDS. The use of MaSDeS in the tissue extraction significantly improves the total number of protein identifications from commonly used tissues, including tissue from the heart, liver, and lung. Notably, MaSDeS significantly enriches membrane proteins, which are often under-represented in proteomics studies. The acid degradable nature of MaSDeS makes it amenable for high-throughput MS-based proteomics. In addition, the thermostability of MaSDeS allows for its use in experiments requiring high temperature to facilitate protein extraction and solubilization. Furthermore, we have shown that MaSDeS outperforms the other MS-compatible surfactants in terms of overall protein solubility and the total number of identified proteins in tissue proteomics. Thus, the use of MaSDeS will greatly advance tissue proteomics and realize its potential in basic biomedical and clinical research. MaSDeS could be utilized in a variety of proteomics studies as well as general biochemical and biological experiments that employ surfactants for protein solubilization.
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