2018
DOI: 10.1021/acs.analchem.8b01638
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The Value of Activated Ion Electron Transfer Dissociation for High-Throughput Top-Down Characterization of Intact Proteins

Abstract: High-throughput top-down proteomic experiments directly identify proteoforms in complex mixtures, making high quality tandem mass spectra necessary to deeply characterize proteins with many sources of variation. Collision-based dissociation methods offer expedient data acquisition but often fail to extensively fragment proteoforms for thorough analysis. Electron-driven dissociation methods are a popular alternative approach, especially for precursor ions with high charge density. Combining infrared photoactiva… Show more

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Cited by 40 publications
(49 citation statements)
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“…Activated-ion electron transfer dissociation (AI-ETD) has rapidly developed as a highly effective tandem MS approach for proteomic applications. [33][34][35][36][37][38][39][40][41] The method uses concurrent infrared (IR) photoactivation to improve dissociation efficiencies and increase product ion generation in electron transfer dissociation (ETD) reactions. 11,42 We report here that the combination of simultaneous vibrational activation from IR photon bombardment and electron-driven dissociation via ETD is particularly well-suited for intact glycopeptide fragmentation.…”
Section: Main Textmentioning
confidence: 99%
See 1 more Smart Citation
“…Activated-ion electron transfer dissociation (AI-ETD) has rapidly developed as a highly effective tandem MS approach for proteomic applications. [33][34][35][36][37][38][39][40][41] The method uses concurrent infrared (IR) photoactivation to improve dissociation efficiencies and increase product ion generation in electron transfer dissociation (ETD) reactions. 11,42 We report here that the combination of simultaneous vibrational activation from IR photon bombardment and electron-driven dissociation via ETD is particularly well-suited for intact glycopeptide fragmentation.…”
Section: Main Textmentioning
confidence: 99%
“…11,12,[21][22][23][24][25][26][13][14][15][16][17][18][19][20] Even with these methods, large-scale analysis of intact glycopeptides remains largely limited to fewer than ~1,000 unique glycosite identifications from any one system or tissue (approximately an order of magnitude behind other PTMs), [27][28][29][30][31][32] and few studies assess heterogeneity across the glycoproteome with site-specific resolution.Activated-ion electron transfer dissociation (AI-ETD) has rapidly developed as a highly effective tandem MS approach for proteomic applications. [33][34][35][36][37][38][39][40][41] The method uses concurrent infrared (IR) photoactivation to improve dissociation efficiencies and increase product ion generation in electron transfer dissociation (ETD) reactions. 11,42 We report here that the combination of simultaneous vibrational activation from IR photon bombardment and electron-driven dissociation via ETD is particularly well-suited for intact glycopeptide fragmentation.…”
mentioning
confidence: 99%
“…By contrast, activated ion-ETD (AI-ETD) uses infrared photoactivation during the ETD reaction to overcome ETnoD, and has been shown to benefit glycoproteomics (Riley et al, 2019), top-down proteomics (McCool et al, 2019;Riley et al, 2018a;Riley et al, 2018b), as well as phosphoproteomics (Riley et al, 2017a). We therefore set out to investigate the utility of AI-ETD on an Orbitrap Fusion Lumos mass spectrometer for identification and confident localization of ADPr sites.…”
Section: Introductionmentioning
confidence: 99%
“…The ability to effectively fragment highly disulfide linked intact proteins with AI-ETD will likely advance efforts towards the structural characterization of many types of proteins such as intact antibodies, toxins, native proteins, and protein complexes. Additionally, AI-ETD was recently shown to benefit top-down characterization of intact proteins in LC-MS/MS analyses, 60 and the work described here lays the groundwork for future experiments that could be conducted on a chromatographic timescale to screen complex mixtures of proteins with intact disulfide bonds. In all, AI-ETD is a superior fragmentation technique for proteins with intact disulfide bonds and will continue to be explored as a tool for disulfide bond analysis in a variety of applications.…”
Section: Resultsmentioning
confidence: 99%