Formation of charged clusters during electrospray ionization of organic solute species

Meng, Can; Fenn, John B.

doi:10.1002/oms.1210260604

Cited by 113 publications

(107 citation statements)

References 11 publications

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“…Pulsed gas cooling allows such a broadband high-resolution FTMS spectrum to be measured every 2 min; summing 10 spectra of recombinant thioredoxin (mMr, 11,667.06, Calbiochem; Fig. 4) lowered the resolution but improved isotopic abundance measurements and retained mass accuracy (measured mMr, 11,667.19).…”

Section: Resultsmentioning

confidence: 99%

“…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), identifying which isotopic peak is the most abundant is compromised by poor abundance accuracy for single scans; the peaks contain only a few ions, and only about three data points are measured per peak in this broadband scan.Pulsed gas cooling allows such a broadband high-resolution FTMS spectrum to be measured every 2 min; summing 10 spectra of recombinant thioredoxin (mMr,11,667.06, Calbiochem; Fig. 4) lowered the resolution but improved isotopic abundance measurements and retained mass accuracy (measured mMr, 11,667.19).…”

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confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

High-resolution tandem mass spectrometry of large biomolecules.

Loo

Quinn

Ryu

et al. 1992

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

120

View full text Add to dashboard Cite

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“…At millimolar concentrations such aggregates can be formed in the electrospray process [176], however, certain peptides are known to self-associate in solution also at much lower concentrations, and these aggregates can also be studied by electrospray ionization. Here two types of such peptides, Aβ-peptides, forming the amyloid plaques intrinsic to Alzheimer's disease pathogenesis, and two tripeptides GPG and ALG shown to inhibit formation of HIV capsids in vitro [177,178] are used to illustrate the applicability of ESI-FTICR mass spectrometry to the study of non-covalent interactions between biomolecules.…”

Section: Methodsmentioning

confidence: 99%

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Palmblad

Bergquist

2003

Journal of Chromatography Library

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Mass spectrometry has in recent years been established as the standard method for protein identification and characterization in proteomics with excellent intrinsic sensitivity and specificity. Fourier transform ion cyclotron resonance is the mass spectrometric technique that provides the highest resolving power and mass accuracy, increasing the amount of information that can be obtained from complex samples. This thesis concerns how useful information on proteins of interest can be extracted from mass spectrometric data on different levels of protein structure and how to obtain this data experimentally. It was shown that it is possible to analyze complex mixtures of protein tryptic digests by direct infusion electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry and identify abundant proteins by peptide mass fingerprinting. Coupling on-line methods such as liquid chromatography and capillary electrophoresis increased the number of proteins that could be identified in human body fluids. Protein identification was also improved by novel statistical methods utilizing prediction of chromatographic behavior and the non-randomness of enzymatic digestion. To identify proteins by short sequence tags, electron capture dissociation was implemented, improved and finally coupled on-line to liquid chromatography for the first time. The combined techniques can be used to sequence large proteins de novo or to localize and characterize any labile post-translational modification. New computer algorithms for the automated analysis of isotope exchange mass spectra were developed to facilitate the study of protein structural dynamics. The non-covalent interaction between HIV-inhibitory peptides and the oligomerization of amyloid β-peptides were investigated, reporting several new findings with possible relevance for development of anti-HIV drug therapies and understanding of fundamental mechanisms in Alzheimer's disease.

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“…This is the [3,16], [Na 3 ϩ (OG) 16 ] 3ϩ cluster with a mass of 4745 Da. Similarly, the lowest mass quadruply charged cluster is [4,27] found at ⌫ ϭ 6¾. At higher mass, sequences with five to ten Na ϩ ions were identified.…”

Section: Example Of Spectramentioning

confidence: 98%

“…Likewise, large, multiply charged clusters with more than one molecule per charge are generated, and this has been referred to as "fractional charging" [27]. The formation of such clusters, as a function of experimental variables, has been a subject of numerous studies [28 -34].…”

Section: Clusters In Esimentioning

confidence: 99%

On the distributions of ion/neutral molecule clusters in electrospray and laser spray—A cluster division model for the electrospray process

Sunner

Beech

Hiraoka

2006

J. Am. Soc. Mass Spectrom.

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The clustering of a medium-sized, involatile, neutral molecule, octyl ␤-D-glucopyranoside (OG), with Na ϩ , Ca 2ϩ , and Yb 3ϩ (M zϩ ) ions in electrospray (ESI) was investigated using laser spray (LSI). 3ϩ , where W represents the water content at the time of dissociation. Based on this study, a cluster division model for electrospray of aqueous solutions of strongly solvated ions is proposed: the Rayleigh droplet disintegration process, which is well-established for the initial stages of electrospray, maintains its general character as it proceeds through a final regime of multiply charged cluster dissociations to the singly and multiply charged ions in mass spectrometry. In the dissociation of multiply charged clusters, the size of each daughter cluster is roughly proportional to the square of the cluster charge. Observed cluster distributions are consistent with a mixture of symmetric and asymmetric cluster dissociations. (J Am Soc Mass Spectrom 2006, 17, 151-162)

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Formation of charged clusters during electrospray ionization of organic solute species

Cited by 113 publications

References 11 publications

High-resolution tandem mass spectrometry of large biomolecules.

High-resolution tandem mass spectrometry of large biomolecules.

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

On the distributions of ion/neutral molecule clusters in electrospray and laser spray—A cluster division model for the electrospray process

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