Physical properties of matrices used for fast atom bombardment

Cook, Kelsey D.; Todd, Peter J.; Friar, Daniel H.

doi:10.1002/bms.1200180708

Cited by 34 publications

(7 citation statements)

References 45 publications

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“…As a consequence, the average lifespan of the ES droplet increases, which in turn causes less evaporative cooling . Thus, m ‐NBA acts as both droplet temperature enhancer and chemical denaturant inside the ES droplet (dielectric constant of m ‐NBA is lower than that of water; see Table ) to unfold or partially unfold the protein, that in turn enhances the charging of the protein . This mechanism is still under controversy because this could not interpret the supercharging of the small analytes such as small organic molecule or peptide, which do not posses any tertiary structure .…”

Section: Resultsmentioning

confidence: 99%

Induction of protein conformational change inside the charged electrospray droplet

Banerjee

2013

J. Mass Spectrom.

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The behavior of the analyte molecules inside the neutral core of the charged electrospray (ES) droplet is not unambiguously known to date. The possibility of protein conformational change inside the charged ES droplet has been investigated. The ES droplets encapsulating the protein molecules were exposed to the acetic acid vapor in the ionization chamber to absorb the acetic acid vapor. Because of the faster evaporation of water than that of acetic acid, the droplets became enriched with acetic acid and thus altered the solvent environment (e.g. pH and polarity) of the final charged droplets from where the naked charged analytes (proteins) are formed. Thus, the perturbation of the ES droplet solvent environment resulted in the protein conformational change (unfolding) during the short lifespan of the ES droplet and that is reflected by the multimodal charge state distribution in the corresponding mass spectra. Further, the extent of this conformational change inside the ES droplet was found to be related to the structural flexibility of the protein. Although the protein conformational change inside the ES droplet has been driven by using acetic acid vapor in the present study, the results would help in the near future to understand the spontaneity of the conformational change of the analyte on the millisecond timescale of phase transition in the natural way of ES process.

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Section: Resultsmentioning

confidence: 99%

Induction of protein conformational change inside the charged electrospray droplet

Banerjee

2013

J. Mass Spectrom.

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“…However, in conjunction with compilations of matrix physical properties (e.g., ref. 46), consideration of data like those in Table 1 should facilitate efforts to rationalize matrix optimization.…”

Section: Discussionmentioning

confidence: 99%

Effect of varying counterions on the sensitivity of electrohydrodynamic and fast atom bombardment mass spectrometry

Reynolds

Cook

1990

J. Am. Soc. Mass Spectrom.

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The abundance of ion pairs (CA+) relative to that of doubly charged ions (C 2 +) in electrohydrodynamic (EH) mass spectra of a series of anions with a common dication in glycerol was found to increase in the order acetate < nitrite < chloride < bromide~ni-trate < iodide < perchlorate. Correlation with enthalpies of hydration for the anions suggests that this trend reflects the solution chemistry of ion association. These spectra also reveal that solvation rather than interactions with the extracting field is more important in determining the overall EH mass spectrometric sensitivity to doubly charged ions. Therefore, the use of anions that promote more extensive ion pairing enhances the overall sensitivity to multiply charged ions that otherwise interact strongly with the solvent, but reduces sensitivity to singly charged ions. These observations hold in fast atom bombardment mass spectrometry, surviving the invasive effects of the primary beam. (J Am Soc Mass Spedrom 1990, 1, 233-237) T h e extreme impact of the choice of solvent [1][2][3][4][5][6][7][8][9] on the appearance of matrix-assisted desorption ionization (DI) mass spectra [10] arises from interacting effects of solvation [11,12], ion pairing [13], surface activity [14,15], mass transport [13,16], and other aspects of solution chemistry. These in turn are convoluted with the effects of primary beam-induced damage intrinsic to most DI experiments [2,3,[17][18][19][20][21][22] and aspects of gas-phase chemistry [23,24]. Although separation of these variables is not generally feasible, an independent understanding of the effects of each would facilitate experimental design for optimum sensitivity. The object of the present study is to isolate the effects of ion pairing on sensitivity in electrohydrodynamic (EH) and fast atom bombardment (FAB) mass spectrometry (MS).Analyte ion-pairing effects have been observed previously in mass spectrometry [14,15,[25][26][27][28][29][30][31]. Although Hand et al. [26] found that counterion effects can be suppressed by use of a liquid matrix, others [14,15,25,[27][28][29][30][31] have explored the use of surface-active counterions to enhance analyte sensitivity. However, such studies have not specifically assessed the extent of ion pairing and its impact on sensitivity.On the basis of evidence of preferential sampling of preformed ions in FAB/MS and EHMS [32,33], it can be predicted that neutralization due to ion pairing of singly charged analytes should decrease sensitivity. The situation is more complex in the case of multi- ply charged ions. Partial charge reduction will decrease solvent-solute interactions, so that the overall sampling efficiency may increase with increased ion pairing, until gains are offset by neutralization. Of course, the effects of beam-induced damage and the possibility of gas-phase ion-molecule reactions subsequent to sampling cloud this picture somewhat.Electrohydrodynamic mass spectrometry [33] provides a means of studying the effects of solution chemistry without interference from an...

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“…In this study several commonly used matrices were tested,8 but it was found that the most abundant molecular ion species [M 2+ − H + ] + and [M 2+ + e − ] +· of porphyrin salts were observed either with SGLY or with NBA. The known electron‐ and especially radical‐acceptor properties of NBA9 were found to be important.…”

Section: Methodsmentioning

confidence: 99%

A fast atom bombardment and matrix‐assisted laser desorption/ionization mass spectrometry study of doubly charged porphyrins

Schäfer

Budzikiewicz

2001

J. Mass Spectrom.

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In this mass spectrometry (MS) study of doubly charged porphyrin salts, fast atom bombardment (FAB) and matrix-assisted laser desorption/ionization (MALDI) MS techniques are utilized to examine several unique ionic species. The predominant transformation of preformed doubly charged ions in the desorption/ionization mechanism of FAB and MALDI is the result of deprotonation reactions to form singly charged ions of the type [M(2+) - H(+)](+) and of one-electron reductions to form radical cations [M(2+) + e(-)](+.). The dependence of this phenomenon and the formation of a number of additional ionic species on the different matrices and the FAB-matrix additive benzoquinone is examined. The significant analogous behavior of doubly charged porphyrins in FAB- and MALDI-MS leads to the conclusion that one-electron reductions are of distinct relevance in the desorption/ionization mechanism of MALDI.

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Physical properties of matrices used for fast atom bombardment

Abstract: Physical and chemical properties of common matrices are tabulated, with aims of facilitating rational matrix selection and providing input for fundamental studies of matrix-assisted ionization. The rationale for selecting tabulated properties is discussed.

Cited by 34 publications

References 45 publications

Induction of protein conformational change inside the charged electrospray droplet

Induction of protein conformational change inside the charged electrospray droplet

Effect of varying counterions on the sensitivity of electrohydrodynamic and fast atom bombardment mass spectrometry

A fast atom bombardment and matrix‐assisted laser desorption/ionization mass spectrometry study of doubly charged porphyrins

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