Fast atom bombardment mass spectrometry: a powerful technique for the study of polar molecules

Williams, Dudley H.; Bradley, Carol V.; Bojesen, Gustav; Santikarn, Sitthivet; Taylor, Lester C. E.

doi:10.1021/ja00409a013

Cited by 262 publications

(61 citation statements)

References 4 publications

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“…(We suggest that this may account for some of the differences between our spectra and those recently reported using fast atom bombardment"..) Decrease in resolution between adjacent peaks of comparable size in a group, resulting from peak broadening, sometimes creates loss of precision in location of peak centroids. This could account for the occasional differences between observed and calculated values in Tables 1 and 2 16 and i.14*16 Only for leu-enkephalin13 can the spectra be directly compared. A number of differences are observed.…”

Section: Discussionmentioning

confidence: 99%

Secondary ion mass spectra of the neuropeptides leucine-enkephalin and methionine-enkephalin

Westmore

Ens

Standing

1982

Biol. Mass Spectrom.

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Positive and negative secondary ion mass spectra obtained by bombardment of thin films of leucine-enkephalin and methionine-enkephalin with a pulsed beam of Cs' ions of energy 5-15 keV were recorded using a time-of-flight mass spectrometer. Many of the secondary ions are metastable. The spectra contain a wealth of information, including the following important features: (i) ions characteristic of the intact molecule, from which the molecular weight may be deduced; (ii) ions diagnostic of the amino acid composition of the peptide; (iii) ions diagnostic of the sequence of amino acids in the peptide.

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Section: Discussionmentioning

confidence: 99%

Secondary ion mass spectra of the neuropeptides leucine-enkephalin and methionine-enkephalin

Westmore

Ens

Standing

1982

Biol. Mass Spectrom.

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“…37) ey reported the formation of sequence-reected fragments such as c-, y-and z+2 ions, corresponding to Biemann's nomenclature, via a hydrogen rearrangement mechanism (Scheme 3). Interestingly, Kenny et al reported that the liquid secondary ion mass spectrum (LSIMS) of a peptide (SALSSSGEE) with a glycerol matrix gave predominantly c-ions originating from N-C α bond cleavage, while the CID of the [M+H] + gave merely b-and y-ions originating from peptide bond cleavage.…”

Section: Observation Of C-ions In Energy-sudden Desorption/ionizationmentioning

confidence: 99%

MALDI In-Source Decay of Protein

Takayama

2016

Mass Spectrometry

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e in-source decay (ISD) phenomenon, the fragmentation at an N-C α bond of a peptide backbone that occurs within several tens of nanoseconds in the ion-source in matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS), is discussed from the standpoints of the discovery and early publications dealing with MALDI-ISD, the formation of c-ions in energy-sudden desorption/ionization methods, the formation of radical species in a MALDI, model construction for ISD, and matrix materials that are suitable for use in MALDI-ISD. e formation of c-ions derived from peptides and proteins in MALDI-ISD can be rationalized by a mechanism involving intermolecular hydrogen transfer, denoted as the "Takayama's model" by De Pauw's group (Anal. Chem. 79: 8678-8685, 2007). It should be emphasized that the model for MALDI-ISD was constructed on the basis of X-ray crystallography and scanning probe microscopy (SPM) analyses of matrix crystals, as well as the use of isotopically-labelled peptides.

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“…A breakthrough was brought about by the advent of particle-induced desorption mass spectrometry [4] and particularly the fast atom bombardment (FAB) [5] technique, which revolutionized the analysis of peptides [6]. Abundant stable ion currents, which also allow the application of the tandem mass spectrometry methods, termed MSMS [7], are usually generated, and the structural characterization of involatile organic compounds using only mass spectrometric means seems now to be feasible [8].…”

mentioning

confidence: 99%

Sequence determination of N-terminal and C-terminal blocked peptides containing N-alkylated amino acids and structure determination of these amino acid constituents by using fast-atom-bombardment/tandem mass spectrometry

et al. 1986

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Peptides, blocked either at the N or C terminus, and thus unsuited for Edman degradation, and those containing N-alkylated amino acids, which are not detectable when using conventional amino acid analysis, can be easily sequenced by applying a method in which fast atom bombardment (FAB) is combined with tandem mass spectrometry (MSMS). Moreover, the structure of the N-alkylated amino acid constituents is provided by this approach. A widely applicable strategy will be presented, and to demonstrate its scope and limitations eighteen analogues of sequences related to the C terminus of substance P, a biologically active neuropeptide, were investigated. The power and reliability of the approach will be demonstrated by analyzing an 'unknown' peptide. Moreover, the detection and structure elucidation of N-alkylated amino acids which usually escape amino acid analysis will be described, as will be the unequivocal differentiation and identification of isomeric MeLeu/ MeIle. The influence of the N-alkylation on the mass spectrometric fragmentation behaviour will be discussed. Furthermore, the sequencing of two adipokinetic hormones by using the combined FAB-MSMS approach is described. Analysis of peptides can be achieved with sample sizes less than 0.1 pmol and be completed within 2-4 h Over the last few years an increasing number of naturally occurring, biologically active peptides was isolated, the sequencing of which was often seriously hampered by the fact that direct application of the Edman degradation was prevented by the presence of a blocked N terminus. Among the many N-protecting groups the N-pyroglutamic acid residue seems to play a pivotal role among the neuropeptide analogues. Furthermore, these peptide analogues often include several types of backbone modifications, among which replacements of various elements, namely the a-carbon, the amide NH group and/or the amide carbonyl, are known [I]. These peptides, in the present context termed modified peptides, were prepared for various reasons such as: a) to confer resistance towards enzymatic degradation which will result in metabolic stability; b) to alter rigidity or flexibility manifested in the normal peptide backbone in order to achieve more potent agonists or change them into antagonists; c) to change chemical and physical properties to effect the pharmacokinetics ; d) to study if the exact alignment and stereochemistry of the peptide backbone are critical for the resulting biologically function;

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Fast atom bombardment mass spectrometry: a powerful technique for the study of polar molecules

Cited by 262 publications

References 4 publications

Secondary ion mass spectra of the neuropeptides leucine-enkephalin and methionine-enkephalin

Secondary ion mass spectra of the neuropeptides leucine-enkephalin and methionine-enkephalin

MALDI In-Source Decay of Protein

Sequence determination of N-terminal and C-terminal blocked peptides containing N-alkylated amino acids and structure determination of these amino acid constituents by using fast-atom-bombardment/tandem mass spectrometry

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