Fragmentation efficiencies of peptide ions following low energy collisional activation

Summerfield, Scott; Gaskell, Simon J.

doi:10.1016/s0168-1176(97)00183-3

Cited by 61 publications

(56 citation statements)

References 41 publications

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“…The contemporary presence in fragment ion y 3 of Arg 8 and Pro 6 at the N-terminal, which usually causes enhanced fragmentation attributed to the greater basicity of prolin substituted nitrogen group [29], can explain the elevated abundance of this fragment in the MRM mode.…”

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confidence: 99%

Qualitative detection of desmopressin in plasma by liquid chromatography–tandem mass spectrometry

et al. 2012

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This work describes a liquid chromatography-electrospray tandem mass spectrometry (LC-ESI-MS/MS) method for detection of desmopressin in human plasma in the low femtomolar range.Desmopressin is a synthetic analogue of the antidiuretic hormone arginine vasopressin and it might be used by athletes as masking agent in the frame of blood passport controls. Therefore, it was recently added by the World Anti-Doping Agency (WADA) to the list of prohibited substances in sport as a masking agent. Mass spectrometry characterization of desmopressin was performed with a high-resolutionOrbitrap-based mass spectrometer. Detection of the peptide in the biological matrix was achieved using a triple quadrupole instrument with an electrospray ionization (ESI) interface after protein precipitation, weak cation solid phase extraction and HPLC separation with an octadecyl reverse phase column. Identification of desmopressin was performed using three product ions, m/z 328.0, m/z 120.0, and m/z 214.0, from the parent ion, m/z 535.5.The extraction efficiency of the method at the limit of detection was estimated at 40% (n=10), the ion suppression at 5% (n=10), and the limit of detection was 50 pg/ml (S/N> 3).Selectivity of the method was verified against several endogenous and synthetic desmopressin related peptides. The performance and the applicability of the method were tested by analysis of clinical samples after administration of desmopressin via intravenous, oral, and intranasal routes. Only after intravenous administration, desmopressin could be successfully detected.3

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confidence: 99%

Qualitative detection of desmopressin in plasma by liquid chromatography–tandem mass spectrometry

et al. 2012

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“…The gas-phase basicity of some peptides was decreased by acetylation: 2% pure acetic anhydride was added to electrospray solution before analysis. Acetylation of different sites was controlled by pH: at slightly acidic pH, only low pKa sites were acetylated, e.g., the N-terminus; at near-neutral pH, intermediate sites were acetylated, e.g., N -Ac of Lys1 in KL 4 KL 4 ; and at basic pH, all sites were acetylated [12].…”

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confidence: 99%

Charge location directs electron capture dissociation of peptide dications

Tsybin

Haselmann

Emmett

et al. 2006

J. Am. Soc. Mass Spectrom.

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The effect of peptide dication charge location on electron capture dissociation (ECD) fragmentation pattern is investigated. ECD fragmentation patterns are compared for peptides with amide and free acid C-terminal groups. ECD of free acid compared with C-terminally amidated peptides with basic residues near the N-terminus demonstrates increased formation of a-type ions. Similarly, ECD of free acid compared with C-terminally amidated peptides with basic residues near the C-terminus exhibits increased formation of y-type ions. Alteration of the peptide sequence to inhibit the formation of charged side chains (i.e., amino acid substitution and acetylation) provides further evidence for charge location effect on ECD. We propose that formation of zwitterionic peptide structures increases the likelihood of amide nitrogen protonation (versus basic side chains), which is responsible for the increase in a-and y-type ion formation. (J Am Soc Mass Spectrom 2006, 17, 1704 -1711

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“…The C-terminal sequence of DIM13 was found to be in agreement with the former internal sequence tags determined from MS 2 spectra. According to the whole MS 2 results, the C-terminal sequence of the DIM13 was identified as (b 14 = 1667.4) -N The DIM13 sequence orientation (N-or C-terminus) deduced by MS 2 was confirmed by carboxypeptidase P treatment and analysis by MALDI-MS. To follow the C-terminus enzymatic sequencing, the kinetics of digestion were established (see Experimental). Figure 3 shows the MALDI mass spectrum from the sequential degradation of DIM13.…”

Section: Resultsmentioning

confidence: 87%

De Novo Sequencing by Nano-Electrospray Multiple-Stage Tandem Mass Spectrometry of An Immune-Induced Peptide of Drosophila Melanogaster

Carte

Cavusoglu

Leize

et al. 2001

Eur J Mass Spectrom (Chichester)

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To combat infection, the fruit fly Drosophila melanogaster responds by rapid synthesis of a series of immune-induced molecules reported as Drosophila immune-induced molecules (DIMs). Characterization of the primary structure of the DIMs is required to establish their exact function. In order to get such information, previous studies on the elucidation of primary structures of the DIMs were developed using a methodology combining matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), highperformance liquid chromatography (HPLC), enzymatic digestion and Edman degradation. Nevertheless, some of the DIMs were resistant to classical Edman sequencing. Therefore, mass spectrometry was used to characterize the primary structure of one of the DIMs, namely the N-blocked DIM13 peptide. The complete sequence of DIM13 was established by means of a strategy of nanoelectrospray ionisation (ESI) combined with multiple-stage tandem mass spectrometry (MS n ) and then was partially confirmed with a combination of enzymatic digestions and MALDI-MS analyses. Interestingly, most of the amino acid sequences have been determined using three-stage (MS 3 ) and four-stage (MS 4 ) tandem experiments, whereas classical tandem mass spectrometry (MS 2 ) yielded only incomplete sequence information. Finally, DIM13 is a 23 amino acid peptide with a pyroglutamic modification at the N terminal position. This work illustrates the remarkable advantages of MS 3 and MS 4 compared with the MS 2 experiment for de novo peptide sequencing. The use of nano-ESI also makes these experiments compatible with the low amount (picomolar level) of DIM13 peptide available for sequencing by ESI-MS n .

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Fragmentation efficiencies of peptide ions following low energy collisional activation

Cited by 61 publications

References 41 publications

Qualitative detection of desmopressin in plasma by liquid chromatography–tandem mass spectrometry

Qualitative detection of desmopressin in plasma by liquid chromatography–tandem mass spectrometry

Charge location directs electron capture dissociation of peptide dications

De Novo Sequencing by Nano-Electrospray Multiple-Stage Tandem Mass Spectrometry of An Immune-Induced Peptide of Drosophila Melanogaster

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