ArticleAnalytical chemistry2014
Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond.Chemical communications (Cambridge, England) · 2023Review
- Composite Multidimensional Ion Mobility-Mass Spectrometry for Improved Differentiation of Stereochemical Modifications.Analytical chemistry · 2023Article
- Mass Spectrometry Approaches Empowering Neuropeptide Discovery and Therapeutics.Pharmacological reviews · 2022Review
- The role of the mobile proton in fucose migration.Analytical and bioanalytical chemistry · 2019Article
- Advances in Mass Spectrometric Tools for Probing Neuropeptides.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015Review
- Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity.Journal of the American Society for Mass Spectrometry · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Peptide sequence scrambling during mass spectrometry-based gas-phase fragmentation analysis causes misidentification of peptides and proteins. Thus, there is a need to develop an efficient approach to probing the gas-phase fragment ion isomers related to sequence scrambling and the underlying fragmentation mechanism, which will facilitate the development of bioinformatics algorithm for proteomics research. Herein, we report on the first use of electron transfer dissociation (ETD)-produced diagnostic fragment ions to probe the components of gas-phase peptide fragment ion isomers. In combination with ion mobility spectrometry (IMS) and formaldehyde labeling, this novel strategy enables qualitative and quantitative analysis of b-type fragment ion isomers. ETD fragmentation produced diagnostic fragment ions indicative of the precursor ion isomer components, and subsequent IMS analysis of b ion isomers provided their quantitative and structural information. The isomer components of three representative b ions (b9, b10, and b33 from three different peptides) were accurately profiled by this method. IMS analysis of the b9 ion isomers exhibited dynamic conversion among these structures. Furthermore, molecular dynamics simulation predicted theoretical drift time values, which were in good agreement with experimentally measured values. Our results strongly support the mechanism of peptide sequence scrambling via b ion cyclization, and provide the first experimental evidence to support that the conversion from molecular precursor ion to cyclic b ion (M → (c)b) pathway is less energetically (or kinetically) favored.
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Registered trials
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