Fast-atom-bombardment-tandem mass spectrometry studies of alkali-metal ions of small peptides

Mallis, Larry M.; Russell, David H.

doi:10.1021/ac00297a021

Cited by 105 publications

(59 citation statements)

References 30 publications

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“…Either the peptide is preferentially cationized at a position close to the tyrosine residue during ionization, or a process of rearrangements occur during CID that promote backbone fragmentation until the cation reaches a position near the tyrosine residue. Tandem mass spectrometry of alkali metal cationized peptides has been described extensively by Gross [40,41], Adams [42,43], Russell [44,45], and Tang [46]. Russell [45] suggested that the sodium ion interacted with the amino terminus or the amide nitrogen in a small tyrosine containing peptide.…”

Section: Resultsmentioning

confidence: 99%

Fragmentation of cationized phosphotyrosine containing peptides by atmospheric pressure MALDI/Ion trap mass spectrometry

Moyer

VonSeggern

Cotter

2003

J. Am. Soc. Mass Spectrom.

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An investigation of phosphate loss from sodium-cationized phosphotyrosine containing peptide ions was conducted using liquid infrared (2.94 m) atmospheric pressure matrixassisted laser desorption/ionization (AP MALDI) coupled to an ion trap mass spectrometer (ITMS). Previous experiments in our laboratory explored the fragmentation patterns of protonated phosphotyrosine containing peptides, which experience a loss of 98 Da under CID conditions in the ITMS. This loss of 98 Da is unexpected for phosphotyrosine, given the structure of its side chain. Phosphate loss from phosphotyrosine residues seems to be dependent on the presence of arginine or lysine residues in the peptide sequence. In the absence of a basic residue, the protonated phosphotyrosine peptides do not undergo losses of HPO 3 (⌬ 80 Da) nor HPO 3 ϩ H 2 O (⌬ 98 Da) in their CID spectra. However, sodium cationized phosphotyrosine containing peptides that do not contain arginine or lysine residues within their sequences do undergo losses of HPO 3 (⌬ 80 Da) and HPO 3 ϩ H 2 O (⌬ 98 Da) in their CID spectra.

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Section: Resultsmentioning

confidence: 99%

Fragmentation of cationized phosphotyrosine containing peptides by atmospheric pressure MALDI/Ion trap mass spectrometry

Moyer

VonSeggern

Cotter

2003

J. Am. Soc. Mass Spectrom.

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“…18 It was therefore decided to study the ESI mass spectra and CID mass spectra of 1 under alkali metal cationization conditions. When LiOH (10 À3 M) was added to the sample and analyzed after allowing it to equilibrate, apart from peaks due to the expected [M Li] ion, peaks arising from multiple lithium exchange were noticed in the spectrum.…”

Section: Resultsmentioning

confidence: 99%

Effect of alkali metal cationization and multiple alkali metal exchange on the collision-induced dissociation of loganic acid studied by electrospray ionization tandem mass spectrometry

Madhusudanan

Raj

Bhaduri

2000

Rapid Commun. Mass Spectrom.

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Under electrospray ionization conditions loganic acid undergoes alkali metal (Li, Na and K) exchange and alkali metal cationization. Multiple exchanges of up to four alkali metal ions are observed. Different populations of metal exchanged species are produced during electrospray ionization. Collision-induced dissociation of ammonium cationized species is compared with that of metal cationized species to study the effect of metal cationization. Glycosidic cleavage and ring cleavages of aglycone and sugar moieties are the major fragmentation pathways observed during collision-induced dissociation. The fragmentations of the highly metal exchanged species indicate the opening of the pyran ring. Collision-induced dissociation of the various metal exchanged and metal cationized species also reveals the nature of the different populations. Copyright 2000 John Wiley & Sons, Ltd.

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“…[6] So far, the majority of the studies have focused on singly charged alkali cationised peptides (some of the examples can be found in Refs. [6][7][8][9][10][11][12][13][14][15][16][17][18]). Collision-induced dissociation (CID) of the singly charged alkali metal cationised peptides led to the sequential loss of amino acids from the C-terminus, i.e.…”

Section: Introductionmentioning

confidence: 99%

Non‐covalent interactions of alkali metal cations with singly charged tryptic peptides

Rožman

Gaskell

2010

J. Mass Spectrom.

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The complexes formed by alkali metal cations (Cat + = Li + ,Na + ,K + ,Rb + ) and singly charged tryptic peptides were investigated by combining results from the low-energy collision-induced dissociation (CID) and ion mobility experiments with molecular dynamics and density functional theory calculations. The structure and reactivity of [M+H +Cat] 2+ tryptic peptides is greatly influenced by charge repulsion as well as the ability of the peptide to solvate charge points. Charge separation between fragment ions occurs upon dissociation, i.e. b ions tend to be alkali metal cationised while y ions are protonated, suggesting the location of the cation towards the peptide N-terminus. The low-energy dissociation channels were found to be strongly dependant on the cation size. Complexes containing smaller cations (Li + or Na + ) dissociate predominantly by sequence-specific cleavages, whereas the main process for complexes containing larger cations (Rb + ) is cation expulsion and formation of [M + H] + . The obtained structural data might suggest a relationship between the peptide primary structure and the nature of the cation coordination shell. Peptides with a significant number of side chain carbonyl oxygens provide good charge solvation without the need for involving peptide bond carbonyl groups and thus forming a tight globular structure. However, due to the lack of the conformational flexibility which would allow effective solvation of both charges (the cation and the proton) peptides with seven or less amino acids are unable to form sufficiently abundant [M+H+Cat] 2+ ion. Finally, the fact that [M+H+Cat] 2+ peptides dissociate similarly as [M + H] + (via sequence-specific cleavages, however, with the additional formation of alkali metal cationised b ions) offers a way for generating the low-energy CID spectra of 'singly charged' tryptic peptides.

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Fast-atom-bombardment-tandem mass spectrometry studies of alkali-metal ions of small peptides

Cited by 105 publications

References 30 publications

Fragmentation of cationized phosphotyrosine containing peptides by atmospheric pressure MALDI/Ion trap mass spectrometry

Fragmentation of cationized phosphotyrosine containing peptides by atmospheric pressure MALDI/Ion trap mass spectrometry

Effect of alkali metal cationization and multiple alkali metal exchange on the collision-induced dissociation of loganic acid studied by electrospray ionization tandem mass spectrometry

Non‐covalent interactions of alkali metal cations with singly charged tryptic peptides

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