ArticleJournal of the American Society for Mass Spectrometry2013
Chemical derivatization of peptide carboxyl groups for highly efficient electron transfer dissociation.
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 16 papers.
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Who cites it
16 citing papers in PubMed.
- Gas Phase Separation of Modified Peptides for Activity-Based Protein Profiling.Analytical chemistry · 2025Article
- Mass Spectrometry Investigation of Some ATP-Binding Cassette (ABC) Proteins.Medicina (Kaunas, Lithuania) · 2024Review
- Recent advances in mass spectrometry analysis of neuropeptides.Mass spectrometry reviews · 2023Review
- Novel Isobaric Tagging Reagent Enabled Multiplex Quantitative Glycoproteomics via Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Catch, Modify and Analyze: Methods of Chemoselective Modification of Cysteine-Containing Peptides.Molecules (Basel, Switzerland) · 2022Review
- Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease.Frontiers in molecular biosciences · 2022Review
- Chemical labeling for fine mapping of IgG N-glycosylation by ETD-MS.Chemical science · 2019Article
- Electron Transfer/Higher Energy Collisional Dissociation of Doubly Charged Peptide Ions: Identification of Labile Protein Phosphorylations.Journal of the American Society for Mass Spectrometry · 2019Article
- Fragmentation of Multi-charged Derivatized Lysine Using Nanospray CID Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Click Chemistry Reagent for Identification of Sites of Covalent Ligand Incorporation in Integral Membrane Proteins.Analytical chemistry · 2017Article
- Solution-phase and solid-phase sequential, selective modification of side chains in KDYWEC and KDYWE as models for usage in single-molecule protein sequencing.New journal of chemistry = Nouveau journal de chimie · 2017Article
- A calibration routine for efficient ETD in large-scale proteomics.Journal of the American Society for Mass Spectrometry · 2015Article
- Cationic Xylene Tag for Increasing Sensitivity in Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2015Article
- O-GlcNAc profiling: from proteins to proteomes.Clinical proteomics · 2014Article
- Proteomic approaches for site-specific O-GlcNAcylation analysis.Bioanalysis · 2014Review
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Authors and funding
7 authors.
Funding
Abstract
The carboxyl groups of tryptic peptides were derivatized with a tertiary or quaternary amine labeling reagent to generate more highly charged peptide ions that fragment efficiently by electron transfer dissociation (ETD). All peptide carboxyl groups-aspartic and glutamic acid side-chains as well as C-termini-were derivatized with an average reaction efficiency of 99 %. This nearly complete labeling avoids making complex peptide mixtures even more complex because of partially-labeled products, and it allows the use of static modifications during database searching. Alkyl tertiary amines were found to be the optimal labeling reagent among the four types tested. Charge states are substantially higher for derivatized peptides: a modified tryptic digest of bovine serum albumin (BSA) generates ~90% of its precursor ions with z > 2, compared with less than 40 % for the unmodified sample. The increased charge density of modified peptide ions yields highly efficient ETD fragmentation, leading to many additional peptide identifications and higher sequence coverage (e.g., 70 % for modified versus only 43 % for unmodified BSA). The utility of this labeling strategy was demonstrated on a tryptic digest of ribosomal proteins isolated from yeast cells. Peptide derivatization of this sample produced an increase in the number of identified proteins, a >50 % increase in the sequence coverage of these proteins, and a doubling of the number of peptide spectral matches. This carboxyl derivatization strategy greatly improves proteome coverage obtained from ETD-MS/MS of tryptic digests, and we anticipate that it will also enhance identification and localization of post-translational modifications.
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