Collision induced dissociation of peptide ions.

Alexander, A. J.; Thibault, Pierre; Boyd, Robert K.; Curtis, Jonathan M.; Rinehart, Kenneth L.

doi:10.1016/0168-1176(90)85012-q

Cited by 66 publications

(35 citation statements)

References 55 publications

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“…Further, for the structural characterisation of unknown compounds, the presence of leucine and isoleucine in the sequence of surfactins makes it necessary to obtain d‐ or w‐ type fragment ions allowing distinction between these two isobaric amino‐acids 11,. 12 We therefore used the sodium‐cationised molecules ([M + Na] + ) in place of the protonated species as precursor ions for the MS/MS experiments.…”

Section: Resultsmentioning

confidence: 99%

Structural investigation of cyclic peptidolipids fromBacillus subtilis by high-energy tandem mass spectrometry

Hue

Sérani

Laprévôte

2001

Rapid Commun. Mass Spectrom.

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The natural products belonging to the surfactin family are cycloheptapeptides bearing a long β‐hydroxy‐fatty acyl chain at the N‐terminal position. The structure of these compounds, often isolated as complex mixtures, can be elucidated by high‐energy tandem mass spectrometry (MS/MS). The protonated molecules generated by cesium ion bombardment (LSIMS) undergo charge‐proximate fragmentations leading to the b‐ and y‐type ion series useful for the sequence determination. The sodium‐cationised molecules show a radically different behaviour towards high‐energy collisional activation. Besides the well‐known charge‐remote dissociation products of the alkyl side chain, complete series of d‐ and w‐type fragments allow easy distinction between leucine and isoleucine. The complementary MS/MS data obtained from the protonated and cationised molecules prove to be of great interest for the structural characterisation of this type of compounds. Copyright © 2001 John Wiley & Sons, Ltd.

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Section: Resultsmentioning

confidence: 99%

Structural investigation of cyclic peptidolipids fromBacillus subtilis by high-energy tandem mass spectrometry

Hue

Sérani

Laprévôte

2001

Rapid Commun. Mass Spectrom.

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“…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.…”

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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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“…For unknowns, however, this multiplicity of isotopically unresolved fragment peaks makes mass assignment from the m/z value seriously ambiguous, as for each mass two or more corresponding peaks of different charge values must be identified. Collisionally activated dissociation (CAD) (3,7,8,(12)(13)(14)(15)(28)(29)(30)(31)(32)(33)(34)(35) of the (M + 10H)1°' peaks of ubiquitin (Fig. 3) gave isotopic peaks whose m/z spacing clearly shows their z values.…”

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“…By using MS/MS (28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39), multiply-charged ESI peptide ions have been dissociated to form some product ions consistent with known sequences for large peptides, even albumin (66 kDa) and IgG (150 kDa) (3,7,8,(12)(13)(14)(15). For unknowns, however, this multiplicity of isotopically unresolved fragment peaks makes mass assignment from the m/z value seriously ambiguous, as for each mass two or more corresponding peaks of different charge values must be identified.…”

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High-resolution tandem mass spectrometry of large biomolecules.

Loo

Quinn

Ryu

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

120

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Unit-resolution mass spectra have been obtained for peptides as large as 17 kDa, providing information on impurities and adduct ions, as well as accurate molecular weight values. Electrospray ionization produces many multiply-charged species of the same mass; isotopic peak resolution provides direct charge state assignment from the unit mass spacing of the isotopes. This is of special value when the spectrum also has many masses, such as from precursor ion dissociation or impurities. Mass measuring errors not only are concomitantly lower (<0.1 Da) than when the isotopic peaks are unresolved but also are independent of variations in '3C/12C natural isotopic abundances. Also, larger errors are avoided that occur when the measured peak envelope includes impurity or adduct ions. This also benefits tandem mass spectrometry; dissociation of peptide ions as large as 8.5 kDa yields fragment masses consistent (<0. (21)(22)(23)(24)(25)(26) can be used to measure simultaneously all such ions as large as 17 kDa with 50,000-80,000 resolving power and, by using an internal standard, with <0.1 Da (<6 ppm) mass errors. As reported here, this enhanced high-resolution capability is also valuable for characterizing impurities (6-8) adducts (9-11) and, by tandem mass spectrometry (MS/MS) (3,7,8,(12)(13)(14)(15), amino acid sequences.EXPERIMENTAL PROCEDURES Radio frequency-only quadrupole lenses and five stages of differential pumping are used to transport the ions electrosprayed at -103 torr to the FTMS ion-measurement cell at <10-8 torr in a 2.8-T magnet. A pulse of N2 gas is admitted to the ion cell to cool the ions translationally before measurement; other experimental details were as given (21-23).RESULTS AND DISCUSSION and the measured value (weighted average of isotopic peak values; external standard: gramicidin S, Mr = 1141) is 12,352.20 (12,358.22 for the most abundant isotopic peak).Note that a 5-per-mil shiftt in the 13C/'2C ratio would change the isotopically averaged molecular weight (centroid of the unresolved isotopic peaks) (1-18) by 0.3 Da but would only affect the abundances of the isotopic peaks, not their masses. These experimental procedures have not produced, to date, high-resolution ESI spectra of molecules as large as albumin (66 kDa), although its spectrum (Fig. 2) was improved (22).By using a quadrupole mass spectrometer (6, 7), the ESI mass spectra of bovine ubiquitin, mMr 8559.62, showed peaks of measured masses 114.7 Da (6) and 115.1 Da (7) below those of the (M + nH)n+ ubiquitin peaks; § this was postulated (7) to result from an impurity missing the two carboxyl-terminal glycines, which would lower the mass by 114.04 Da. The ESI/FTMS mass spectrum of the same sample (7) (Fig. 3) shows an mMr of 8559.45 and peaks presumably from the same impurity at a mMr of 8445.43 (Am = 114.02). Additional anomalous peaks not resolved in the quadrupole spectra (6,7) give an average mMr of 8623.39 (Am = 63.94); replacing a valine by a tyrosine would increase the molecular weight by 63.99. As noted (23), ident...

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Collision induced dissociation of peptide ions.

Cited by 66 publications

References 55 publications

Structural investigation of cyclic peptidolipids fromBacillus subtilis by high-energy tandem mass spectrometry

Structural investigation of cyclic peptidolipids fromBacillus subtilis by high-energy tandem mass spectrometry

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

High-resolution tandem mass spectrometry of large biomolecules.

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