Fast atom bombardment and tandem mass spectrometry of synthetic nucleopeptides

Waghmare, S. V.; Fokkens, Roel H.; Nibbering, Nico M. M.; Kuyl‐Yeheskiely, E.; Boom, Jacques H. van

doi:10.1002/bms.1200200906

Cited by 2 publications

(1 citation statement)

References 26 publications

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“…This enabled not only to identify the main building blocks, but also to sequence their peptide part. The cleavage of the peptide‐phosphate backbone occurred mainly via a 1,5‐H shift from the side chain of the neighboring amino acid to the oxygen phosphate and the number of amino acids present in the peptide part was found to have influence on the location of sodium ion cationization (Waghmare et al, 1991). The same strategy was applied in a subsequent study to verify the position of the phosphate group in some cyclic and linear synthetic phosphopeptides.…”

Section: Miscellaneousmentioning

confidence: 99%

Four decades of joy in mass spectrometry

Nibbering

2006

Mass Spectrometry Reviews

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Tremendous developments in mass spectrometry have taken place in the last 40 years. This holds for both the science and the instrumental revolutions in this field. In chemistry the research was heavily focused on organic molecules that upon electron ionization fragmented via complex mechanistic pathways as shown by isotopic labeling experiments. These studies, including ion structure determinations, were performed with use of double focusing mass spectrometers of both conventional and reversed geometry, and equipped with various types of metastable ion scanning and collision-induced dissociation techniques developed by physical and analytical chemists. Time-resolved mass spectrometry by use of the field ionization kinetics method, developed by physical chemists, was another powerful way to unravel details of unimolecular gas phase ion dissociations. Then the development of new ionization methods, such as desorption chemical ionization, field desorption, and fast atom bombardment permitted not only to analyze unvolatile, thermally labile and higher molecular weight compounds, but also to study their chemical behavior in the gas phase, initially with use of double focusing instruments and later on with multisector and hybrid mass spectrometers. These ionization methods also enabled to study organometallic compounds and increasingly the field of medium-sized to large biomolecules, the latter being exploded in the last decade by the development of electrospray- and matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. Another area of research concerned the bimolecular chemistry of organic ions with organic molecules in the gas phase. Initially this was performed with use of among others drift-cell ion cyclotron resonance spectroscopy, that later on was replaced by the developed method of ion trapping and Fourier transform ion cyclotron resonance. Combination of the latter with the afore-mentioned ionization methods has shifted also in this case the research on organic molecules to organometallic/inorganic systems, and predominantly to biomolecules in the last decade. This invited review will describe the research efforts made by the author's group over the last 40 years together with some personal experiences during his career.

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Section: Miscellaneousmentioning

confidence: 99%

Four decades of joy in mass spectrometry

Nibbering

2006

Mass Spectrometry Reviews

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Verification of the position of the phosphate group in some synthetic phosphopeptides by fast‐atom bombardment and tandem mass spectrometry

Nijenhuis

Fokkens

Nibbering

et al. 1993

Rapid Comm Mass Spectrometry

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Some synthetically obtained linear and cyclic phosphopeptides of low molecular weight have been studied by fast-atom bombardment and tandem mass spectrometry to verify the position of the phosphate group in these compounds. Based upon the occurrence/non-occurrence of loss of phosphoric acid from low abundance fragment ions induced by low-and high-energy collisions with target gases, it is shown that the position of the phosphate group in the phosphopeptides studied can be determined unequivocally.The development of soft ionization methods such as field desorption (FD),' fast-atom bombardment (FAB) ,* laser desorption (LD)3 and electrospray (ES)4has enabled the analysis of peptide? in the solid phase or in solution without the need for prior derivatization. The corresponding mass spectra usually contain large peaks due to the protonated or cationized molecules and therefore are very suited for providing the molecular weights of peptides. However, the reduced extent of fragmentation and, as a consequence, small fragmention peaks in such spectra make it more difficult to obtain the amino acid sequence of the peptides. The latter problem can be overcome by the use of tandem mass spectrometry (MS/MS) in conjunction with collision-induced dissociation (CID) to promote fragmentation useful for the structure elucidation of peptides.6 In this paper the analyses of several synthetic linear and cyclic phosphopeptides by FAB-MS and FAB-MS/MS are reported as an extension of our earlier papers7,' on the sequence analysis of synthetic nucleopeptides and deuterium-labelled peptides. It will be shown that it is possible to determine unequivocally the position of the phosphate group in the synthetic phosphopeptides by application of FAB-MS/MS. EXPERIMENTAL InstrumentsThe spectra were recorded by use of a ZAB-HFqQ mass spectrometer (VG Analytical, Manchester, UK) with the configuration BEqQ (B =magnetic sector, E = electric sector, q = R F only quadrupole, Q = quadrupole mass filter) which was coupled to a VG 11/250 data system. For obtaining the full-scan FAB spectra, the phosphopeptides were dissolved in thioglycerol (concentration 1 mmol/L), loaded on a stainless steel probe and bombarded with xenon atoms having 8 keV kinetic energy. For the acquisition of the FAB/MIKE (mass-analyzed ion kinetic energy) and

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Fast atom bombardment and tandem mass spectrometry of synthetic nucleopeptides

Cited by 2 publications

References 26 publications

Four decades of joy in mass spectrometry

Four decades of joy in mass spectrometry

Verification of the position of the phosphate group in some synthetic phosphopeptides by fast‐atom bombardment and tandem mass spectrometry

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