FAB and tandem mass spectrometry of synthetic neuropeptides and their2H-labelled analogues

Waghmare, S. V.; Fokkens, Roel H.; Nibbering, Nico M. M.; Kaspersen, Frans M.

doi:10.1002/bms.1200180930

Cited by 4 publications

(2 citation statements)

References 14 publications

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“…trometry in determining the amino acid sequence of labeled peptides was investigated (234). Sulfur-containing deuterated and nondeuterated Org 2766 59, as well as ACTH (235) neuropeptides were used as analytes.…”

Section: (93)mentioning

confidence: 99%

Mass spectrometry of sulfur‐containing compounds in organic and bioorganic fields

Bortolini¹,

Fogagnolo²

1995

Mass Spectrometry Reviews

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This survey covers the mass spectrometic properties of organosulfur compounds containing the sulfide, disulfide, and sulfone functional groups. Attention is paid to the uni‐ and biomolecular chemistry of both positive and negative ions, as well as to the reactions of ions, with sulfur containing species, in the gas phase. The role of other functional groups on the decomposition of organic S, SO, SO2 containing gaseous ions is also discussed. The selection of sulfur containing compounds includes many naturally occurring and pharmaceutically significant products, that will be presented in the following order: alkaloids, amino acids, peptides, proteins, carbohydrates, steroids, and metabolites. © 1996 John Wiley & Sons, Inc.

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Section: (93)mentioning

confidence: 99%

Mass spectrometry of sulfur‐containing compounds in organic and bioorganic fields

Bortolini¹,

Fogagnolo²

1995

Mass Spectrometry Reviews

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“…In cooperation with the Dutch pharmaceutical company mentioned the amino acid sequence of a synthetic neuropeptide, and its deuterium labeled analogs was verified by use of fast atom bombardment and tandem mass spectrometry. The spectra showed predominantly peaks due to N ‐terminal sequence ions and some peaks due to C ‐terminal sequence ions and permitted to determine the amount and the position of deuterium incorporated in the peptide (Waghmare et al, 1989). Similarly, in cooperation with Professor J.H.…”

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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Fast atom bombardment and tandem mass spectrometry of synthetic nucleopeptides

Waghmare

Fokkens

Nibbering

et al. 1991

Biol. Mass Spectrom.

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Positive pod negative ion fast atom bombardment (FAB) combined with tandem mass spectrometry (MS/MS) has been used to sequence four f a y protected nucleopeptides. Protomted and deprotonated molecules and some structurally signi6cant fragments, predominantly sodium cationized/decatidzed adducts, are observed. The tandem mass spectra of the protonated/deprotonated molecules help to identify (bidirectionally) the main building Mocks rod the sequence ions of the peptide part of the nucleopeptide components. It is fouod that the cleavage of the peptide-phosphate backbone mainly occurs due to 1,SH shift from the side chain of the neighbouring amino acid to the oxygen of the phosphate. It is also observed that the number of amino acids present in the peptide part has a potential influence on the location of the cationization (Na') which in turn influences the fragmentation pattern in the mass spectrometer.

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FAB and tandem mass spectrometry of synthetic neuropeptides and their2H-labelled analogues

Cited by 4 publications

References 14 publications

Mass spectrometry of sulfur‐containing compounds in organic and bioorganic fields

Mass spectrometry of sulfur‐containing compounds in organic and bioorganic fields

Four decades of joy in mass spectrometry

Fast atom bombardment and tandem mass spectrometry of synthetic nucleopeptides

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