ArticleJournal of the American Society for Mass Spectrometry2013
On-line electrochemical reduction of disulfide bonds: improved FTICR-CID and -ETD coverage of oxytocin and hepcidin.
Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Spatially Selective Electrochemical Cleavage of a Polymerase-Nucleotide Conjugate.ACS synthetic biology · 2023Article
- Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins.The Analyst · 2022Article
- Characterization of Protein Disulfide Linkages by MS In-Source Dissociation Comparing to CID and ETD Tandem MS.Journal of the American Society for Mass Spectrometry · 2019Article
- Top-Down Characterization of Proteins with Intact Disulfide Bonds Using Activated-Ion Electron Transfer Dissociation.Analytical chemistry · 2018Article
- Structure elucidation and quantification of the reduction products of anticancer Pt(iv) prodrugs by electrochemistry/mass spectrometry (EC-MS).The Analyst · 2018Article
- In-Depth Characterization of Protein Disulfide Bonds by Online Liquid Chromatography-Electrochemistry-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry.International journal of mass spectrometry · 2015Article
- Characterization of cyclic peptides containing disulfide bonds.Journal of pharmaceutical and biomedical analysis · 2015Article
- Integration of electrochemistry with ultra-performance liquid chromatography/mass spectrometry.European journal of mass spectrometry (Chichester, England) · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Particularly in the field of middle- and top-down peptide and protein analysis, disulfide bridges can severely hinder fragmentation and thus impede sequence analysis (coverage). Here we present an on-line/electrochemistry/ESI-FTICR-MS approach, which was applied to the analysis of the primary structure of oxytocin, containing one disulfide bridge, and of hepcidin, containing four disulfide bridges. The presented workflow provided up to 80% (on-line) conversion of disulfide bonds in both peptides. With minimal sample preparation, such reduction resulted in a higher number of peptide backbone cleavages upon CID or ETD fragmentation, and thus yielded improved sequence coverage. The cycle times, including electrode recovery, were rapid and, therefore, might very well be coupled with liquid chromatography for protein or peptide separation, which has great potential for high-throughput analysis.
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Registered trials
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