ArticleJournal of the American Society for Mass Spectrometry2012
Photodissociation of charge tagged peptides.
Article in Journal of the American Society for Mass Spectrometry, 2012. 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.
- Diagnostic utility of N-terminal TMPP labels for unambiguous identification of clipped sites in therapeutic proteins.Scientific reports · 2023Article
- Analysis of Fragmentation Pathways of Peptide Modified with Quaternary Ammonium and Phosphonium Group as Ionization Enhancers.Molecules (Basel, Switzerland) · 2021Article
- Identification of N-terminal protein processing sites by chemical labeling mass spectrometry.Rapid communications in mass spectrometry : RCM · 2019Article
- A Novel Triethylphosphonium Charge Tag on Peptides: Synthesis, Derivatization, and Fragmentation.Journal of the American Society for Mass Spectrometry · 2017Article
- Distinguishing Aspartic and Isoaspartic Acids in Peptides by Several Mass Spectrometric Fragmentation Methods.Journal of the American Society for Mass Spectrometry · 2016Article
- Charge transfer dissociation (CTD) mass spectrometry of peptide cations using kiloelectronvolt helium cations.Journal of the American Society for Mass Spectrometry · 2014Article
- Photodissociation mass spectrometry: new tools for characterization of biological molecules.Chemical Society reviews · 2014Review
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Authors and funding
4 authors.
Funding
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Abstract
Tris(2,4,6-trimethoxyphenyl) phosphonium acetyl (TMPP-Ac) was previously introduced to improve the mass spectrometric sequence analysis of peptides by fixing a permanent charge at the N-termini. However, peptides containing arginine residues did not fragment efficiently after TMPP-Ac modification. In this work, we combine charge derivatization with photodissociation. The fragmentation of TMPP-derivatized peptides is greatly improved and a series of N-terminal fragments is generated with complete sequence information. Arginine has a special effect on the fragmentation of the TMPP tagged peptides when it is the N-terminal peptide residue. Theoretical and experimental results suggest that this is due to hydrogen transfer from the charged N-terminus to the hydrogen-deficient peptide sequence.
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Registered trials
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