ArticleJournal of the American Society for Mass Spectrometry2009
The role of amino acid composition in the charge inversion of deprotonated peptides via gas-phase ion/ion reactions.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Sequencing of Phosphopeptides Using a Sequential Charge Inversion Ion/Ion Reaction and Electron Capture Dissociation Workflow.Journal of the American Society for Mass Spectrometry · 2024Article
- Reagent cluster anions for multiple gas-phase covalent modifications of peptide and protein cations.Journal of the American Society for Mass Spectrometry · 2013Article
- Gas-phase ion/ion reactions of peptides and proteins: acid/base, redox, and covalent chemistries.Chemical communications (Cambridge, England) · 2013Article
- Covalent and non-covalent binding in the ion/ion charge inversion of peptide cations with benzene-disulfonic acid anions.Journal of mass spectrometry : JMS · 2012Article
- Dissociation Behavior of Tryptic and Intramolecular Disulfide-linked Peptide Ions Modified in the Gas Phase via Ion/Ion Reactions.International journal of mass spectrometry · 2012Article
- Transmission mode ion/ion reactions in the radiofrequency-only ion guide of hybrid tandem mass spectrometers.Rapid communications in mass spectrometry : RCM · 2009Article
- Mass spectrometry of dendrimers.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ion/ion charge inversion via multiple proton transfer reactions occurs via a long-lived intermediate. The intermediate can be observed if its lifetime is long relative to mechanisms for removal of excess energy (i.e., emission and collisional stabilization). The likelihood for formation of a stabilized intermediate is a function of characteristics of the reagent and analyte ions. This work is focused on the role acidic and basic sites of a deprotonated peptide play in the formation of a stabilized intermediate upon charge inversion with multiply protonated polypropyleniminediaminobutane dendrimers. A group of model peptides based on leucine enkephalin was used, which included YGGFL, YGGFLF, YGGFLK, YGGFLR and YGGFLH as well as methyl esterified and acetylated versions. Results showed that peptides containing basic amino acid residues charge inverted primarily by proton transfer from the DAB dendrimer to the peptide, whereas peptides without basic amino acids charge inverted primarily by complex formation with the DAB dendrimer. The modified versions of the peptides highlighted the importance of the presence of the C-terminus as well as the basicity of the peptide in the observation of a stabilized intermediate. These results provide new insights into the nature of the interactions that occur in the charge inversion of polypeptide anions via ion/ion reactions.
Indexed as
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Registered trials
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