ArticleChemical science2020
Fast protein analysis enabled by high-temperature hydrolysis.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Microfluidics for the biological analysis of atmospheric ice-nucleating particles: Perspectives and challenges.Biomicrofluidics · 2025Review
- Sample transformation in online separations: how chemical conversion advances analytical technology.Chemical communications (Cambridge, England) · 2023Review
- Easy, Robust, and Repeatable Online Acid Cleavage of Proteins in Mobile Phase for Fast Quantitative LC-MS Bottom-Up Protein Analysis─Application for Ricin Detection.Analytical chemistry · 2023Article
- Investigation of Tryptic Protein Digestion in Microdroplets and in Bulk Solution.Journal of the American Society for Mass Spectrometry · 2022Article
- Recent advances in on-site mass spectrometry analysis for clinical applications.Trends in analytical chemistry : TRAC · 2022Review
- Peptide and protein assays using customizable bio-affinity arrays combined with ambient ionization mass spectrometry.Chemical science · 2021Article
- Microdroplet Ultrafast Reactions Speed Antibody Characterization.Analytical chemistry · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While the bottom-up protein analysis serves as a mainstream method for biological studies, its efficiency is limited by the time-consuming process for enzymatic digestion or hydrolysis as well as the post-digestion treatment prior to mass spectrometry analysis. In this work, we developed an enzyme-free microreaction system for fast and selective hydrolysis of proteins, and a direct analysis of the protein digests was achieved by nanoESI (electrospray ionization) mass spectrometry. Using the microreactor, proteins in aqueous solution could be selectively hydrolyzed at the aspartyl sites within 2 min at high temperatures (∼150 °C). Being free of salts, the protein digest solution could be directly analyzed using a mass spectrometer with nanoESI without further purification or post-digestion treatment. This method has been validated for the analysis of a variety of proteins with molecular weights ranging from 8.5 to 67 kDa. With introduction of a reducing agent into the protein solutions, fast cleavage of disulfide bonds was also achieved along with high-temperature hydrolysis, allowing for fast analysis of large proteins such as bovine serum albumin. The high-temperature microreaction system was also used with a miniature mass spectrometer for the determination of highly specific peptides from
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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.