Electron Induced Dissociation of Singly Deprotonated Peptides

Kalli, Anastasia; Grigorean, Gabriela; Håkansson, Kristina

doi:10.1007/s13361-011-0233-6

Cited by 25 publications

(36 citation statements)

References 72 publications

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“…Here, we use the term electron induced dissociation (EID) to describe the fragmentation observed upon electron irradiation of the molecular ions with high energy (910 eV) electrons. EID is more often employed for the fragmentation of singly charged species, including protonated amino acids [56], protonated peptides [54,56,57], protonated and sodiated betaine dimers [58], oligosaccharides [59], metalated fatty acids [60], oxo-centered trinuclear carboxylate-bridged iron complexes [61], deprotonated peptides [62], metabolites [63], and glycosaminoglycans [64]. More recently EID has also been applied for dissociation of multiply charged species in both positive [54,65,66] and negative [67] ion mode.…”

Section: + H] 2+· and [M -2h]mentioning

confidence: 99%

Fragmentation of Singly, Doubly, and Triply Charged Hydrogen Deficient Peptide Radical Cations in Infrared Multiphoton Dissociation and Electron Induced Dissociation

Kalli

Hess

2011

J. Am. Soc. Mass Spectrom.

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Section: + H] 2+· and [M -2h]mentioning

confidence: 99%

Fragmentation of Singly, Doubly, and Triply Charged Hydrogen Deficient Peptide Radical Cations in Infrared Multiphoton Dissociation and Electron Induced Dissociation

Kalli

Hess

2011

J. Am. Soc. Mass Spectrom.

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“…The application of electron‐based dissociation techniques for singly charged gaseous ions, referred here as EID, has received notable interest of late but has a rich history dating back to the work of Cody and Freiser . We present the use of EID to structurally characterize PC ions produced via matrix‐assisted laser desorption ionization (MALDI) on a Fourier transform ion cyclotron resonance (FT‐ICR) mass spectrometer.…”

Section: Introductionmentioning

confidence: 99%

Electron‐induced dissociation (EID) for structure characterization of glycerophosphatidylcholine: determination of double‐bond positions and localization of acyl chains

et al. 2015

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Glycerophospholipids are a highly abundant and diverse collection of biologically relevant lipids and distinction between isomeric and isobaric species is a fundamental aspect for confident identification. The ability to confidently assign a unique structure to a glycerophospholipid of interest is dependent on determining the number and location of the points of unsaturation and assignment of acyl chain position. The use of high energy electrons (>20 eV) to induce gas-phase dissociation of intact precursor ions results in diagnostic product ions for localizing double bond positions and determining acyl chain assignment. We describe a high resolution, tandem mass spectrometry method for structure characterization of glycerophospholipids using electron-induced dissociation (EID). Furthermore, the inclusion of nomenclature to systematically assign bond cleavage sites with acyl chain position and double bond location enables a uniform platform for lipid identification. The EID methodology detailed here combines novel application of an electron-based dissociation technique with high resolution mass spectrometry that facilitates a new experimental approach for lipid biomarker discovery and validation.

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“…2,3 Compared to CID or IRMPD, electron capture dissociation (ECD) [4][5][6][7] and electron transfer dissociation (ETD) 8,9 of multiply-charged peptide/protein cations typically produce spectra with greater sequence coverage and PTM localisation, due to extensive, non-selective fragmentation. 9,10 Electron-induced dissociation (EID) of both protonated 11,12 and deprotonated 13 singly charged peptide ions also elicits additional radical driven sequence coverage information complementary to that derived from collisional activation, without modifying the initial charge state.…”

Section: Introductionmentioning

confidence: 99%

Photodissociation of TEMPO-modified peptides: new approaches to radical-directed dissociation of biomolecules

Marshall

Hansen

Trevitt

et al. 2014

Phys. Chem. Chem. Phys.

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Photodissociation of TEMPO-modified peptides: new approaches to radical-directed dissociation of biomolecules AbstractRadical-directed dissociation of gas phase ions is emerging as a powerful and complementary alternative to traditional tandem mass spectrometric techniques for biomolecular structural analysis. Previous studies have identified that coupling of 2-[(2,2,6,6-tetramethylpiperidin-1-oxyl)methyl]benzoic acid (TEMPO-Bz) to the N-terminus of a peptide introduces a labile oxygen-carbon bond that can be selectively activated upon collisional activation to produce a radical ion. Here we demonstrate that structurally-defined peptide radical ions can also be generated upon UV laser photodissociation of the same TEMPO-Bz derivatives in a linear ion-trap mass spectrometer. When subjected to further mass spectrometric analyses, the radical ions formed by a single laser pulse undergo identical dissociations as those formed by collisional activation of the same precursor ion, and can thus be used to derive molecular structure. Mapping the initial radical formation process as a function of photon energy by photodissociation action spectroscopy reveals that photoproduct formation is selective but occurs only in modest yield across the wavelength range (300-220 nm), with the photoproduct yield maximised between 235 and 225 nm. Based on the analysis of a set of model compounds, structural modifications to the TEMPO-Bz derivative are suggested to optimise radical photoproduct yield. Future development of such probes offers the advantage of increased sensitivity and selectivity for radicaldirected dissociation. AbstractRadical-directed dissociation of gas phase ions is emerging as a powerful and complementary alternative to traditional tandem mass spectrometric techniques for biomolecular structural analysis. Previous studies have identified that coupling of 2-[(2,2,6,6-tetramethylpiperidin-1-oxyl)methyl]benzoic acid (TEMPO-Bz) to the N-terminus of a peptide introduces a labile oxygen-carbon bond that can be selectively activated upon collisional activation to produce a radical ion. Here we demonstrate that structurally-defined peptide radical ions can also be generated upon UV laser photodissociation of the same TEMPO-Bz derivatives in a linear ion-trap mass spectrometer. When subjected to further mass spectrometric analyses, the radical ions formed by a single laser pulse undergo identical dissociations as those formed by collisional activation of the same precursor ion, and can thus be used to derive molecular structure. Mapping the initial radical formation process as a function of photon energy by photodissociation action spectroscopy reveals that photoproduct formation is selective but occurs only in modest yield across the wavelength range (300 -220 nm), with the photoproduct yield maximised between 235 and 225 nm. Based on the analysis of a set of model compounds, structural modifications to the TEMPO-Bz derivative are suggested to optimise radical photoproduct yield. Future development of such probes offers t...

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Electron Induced Dissociation of Singly Deprotonated Peptides

Cited by 25 publications

References 72 publications

Fragmentation of Singly, Doubly, and Triply Charged Hydrogen Deficient Peptide Radical Cations in Infrared Multiphoton Dissociation and Electron Induced Dissociation

Fragmentation of Singly, Doubly, and Triply Charged Hydrogen Deficient Peptide Radical Cations in Infrared Multiphoton Dissociation and Electron Induced Dissociation

Electron‐induced dissociation (EID) for structure characterization of glycerophosphatidylcholine: determination of double‐bond positions and localization of acyl chains

Photodissociation of TEMPO-modified peptides: new approaches to radical-directed dissociation of biomolecules

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