ArticleJournal of the American Society for Mass Spectrometry2011
Intra- and inter-molecular cross-linking of peptide ions in the gas phase: reagents and conditions.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Structural differentiation of protein charge state conformers via gas-phase ion/ion cross-linking mass spectrometry.International journal of mass spectrometry · 2025Article
- Imaging Mass Spectrometry of Sulfatide Isomers from Rat Brain Tissue Using Gas-Phase Charge Inversion Ion/Ion Reactions.Journal of the American Society for Mass Spectrometry · 2025Article
- Structural Elucidation and Relative Quantification of Fatty Acid Double Bond Positional Isomers in Biological Tissues Enabled by Gas-Phase Charge Inversion Ion/Ion Reactions.Analysis & sensing · 2024Article
- Relative Quantification of Lipid Isomers in Imaging Mass Spectrometry Using Gas-Phase Charge Inversion Ion/Ion Reactions and Infrared Multiphoton Dissociation.Analytical chemistry · 2023Article
- Perspective on Emerging Mass Spectrometry Technologies for Comprehensive Lipid Structural Elucidation.Analytical chemistry · 2021Article
- C-terminal peptide extension via gas-phase ion/ion reactions.International journal of mass spectrometry · 2015Article
- Gas-Phase Amidation of Carboxylic Acids with Woodward's Reagent K Ions.Journal of the American Society for Mass Spectrometry · 2015Article
- Transformation of [M + 2H](2+) Peptide Cations to [M - H](+), [M + H + O](+), and M(+•) Cations via Ion/Ion Reactions: Reagent Anions Derived from Persulfate.Journal of the American Society for Mass Spectrometry · 2015Article
- Ion/ion reactions with "onium" reagents: an approach for the gas-phase transfer of organic cations to multiply-charged anions.Journal of the American Society for Mass Spectrometry · 2015Article
- Gas phase reactivity of carboxylates with N-hydroxysuccinimide esters.Journal of the American Society for Mass Spectrometry · 2015Article
- Oxidation of methionine residues in polypeptide ions via gas-phase ion/ion chemistry.Journal of the American Society for Mass Spectrometry · 2014Article
- Efficient and directed peptide bond formation in the gas phase via ion/ion reactions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Gas Phase Dissociation Behavior of Acyl-Arginine Peptides.International journal of mass spectrometry · 2013Article
- Strategies for the Gas Phase Modification of Cationized Arginine via Ion/ion Reactions.International journal of mass spectrometry · 2013Article
- 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 intramolecular protein crosslinking via ion/ion reactions: ubiquitin and a homobifunctional sulfo-NHS ester.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
- Gas-phase reactivity of carboxylic acid functional groups with carbodiimides.Journal of the American Society for Mass Spectrometry · 2013Article
- 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
- Solution versus gas-phase modification of peptide cations with NHS-ester reagents.Journal of the American Society for Mass Spectrometry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Intra-molecular and inter-molecular cross-linking of protonated polypeptide ions in the gas phase via ion/ion reactions have been demonstrated using N-hydroxysulfosuccinimide (sulfo-NHS)- based reagent anions. The initial step in the ion/ion reaction involves the formation of a long-lived complex between the peptide and reagent, which is a prerequisite for the covalent bioconjugation chemistry. The sulfonate groups on the NHS rings of the homo-bifunctional cross-linking reagents have high affinity for the protonated sites in the peptide and, therefore, facilitate the long-lived complex formation. In addition to the formation of a long-lived chemical complex, intra-molecular cross-linking also requires two unprotonated primary amine sites within a molecule where the covalent modification takes place. Alternatively, inter-molecular cross-linking demands the availability of one neutral primary amine site in each of the two peptides that are being cross-linked. Nucleophilic displacement of two sulfo-NHS groups by the amine functionalities in the peptide is a signature of the covalent cross-linking chemistry in the gas phase. Upon removal of the two sulfo-NHS groups, two amide bonds are formed between an unprotonated, primary amine group of a lysine side chain in the peptide and the carboxyl group in the reagent.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.