ArticleJournal of the American Society for Mass Spectrometry2013
Collision-induced dissociation fragmentation inside disulfide C-terminal loops of natural non-tryptic peptides.
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 6 papers.
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Who cites it
6 citing papers in PubMed.
- ExD identification of C-terminal Ile/Leu in natural peptides using d-ions.Analytical and bioanalytical chemistry · 2026Article
- The Road to the Full Sequencing of Natural Frogs' Peptides Relying Solely on Mass Spectrometry.Mass spectrometry (Tokyo, Japan) · 2025Review
- Mass Spectrometric De Novo Sequencing of Natural Peptides.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Tandem Mass Spectrometry de novo Sequencing of the Skin Defense Peptides of the Central Slovenian Agile FrogMolecules (Basel, Switzerland) · 2023Article
- Differentiation of Central Slovenian and Moscow populations of Rana temporaria frogs using peptide biomarkers of temporins family.Analytical and bioanalytical chemistry · 2021Article
- Article
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Authors and funding
7 authors.
Funding
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Abstract
Collision-induced dissociation (CID) spectra of long non-tryptic peptides are usually quite complicated and rather difficult to interpret. Disulfide bond formed by two cysteine residues at C-terminus of frog skin peptides precludes one to determine sequence inside the forming loop. Thereby, chemical modification of S-S bonds is often used in "bottom up" sequencing approach. However, low-energy CID spectra of natural non-tryptic peptides with C-terminal disulfide cycle demonstrate an unusual fragmentation route, which may be used to elucidate the "hidden" C-terminal sequence. Low charge state protonated molecules experience peptide bond cleavage at the N-terminus of C-terminal cysteine. The forming isomeric acyclic ions serve as precursors for a series of b-type ions revealing sequence inside former disulfide cycle. The reaction is preferable for peptides with basic lysine residues inside the cycle. It may also be activated by acidic protons of Asp and Glu residues neighboring the loop. The observed cleavages may be quite competitive, revealing the sequence inside disulfide cycle, although S-S bond rupture does not occur in this case.
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