Detection of mass 16241 ions by Fourier-transform mass spectrometry

Castro, Mauro E.; Russell, David H.; Amster, I. Jonathan; McLafferty, Fred W.

doi:10.1021/ac00293a049

Cited by 41 publications

(13 citation statements)

References 34 publications

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“…They also display signal enhancement due to constructive overlap, , with corresponding m / z values 7667.5, 8706.8, 12 863.9, 16 241.8, and 19 359.8. This spectrum is highly consistent with those previously reported on Q-ToF ,, and Orbitrap systems and historically, on a 3 T FT-ICR-MS instrument . However, ions above m / z 20 000, as previously reported by Lebrilla et al are not observed.…”

Section: Resultssupporting

confidence: 92%

“…This spectrum is highly consistent with those previously reported on Q-ToF 24,29,55 and Orbitrap 36 systems and historically, on a 3 T FT-ICR-MS instrument. 56 However, ions above m/z 20 000, as previously reported by Lebrilla et al 57 are not observed. Since the instrument described herein is commercial, it is possible enhancements may be required to improve ultrahigh m/z transmission, such as increased source pressure for improved collisional cooling and ion transmission of the larger CsI clusters.…”

Section: ■ Results and Discussionmentioning

confidence: 68%

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High Mass Analysis with a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: From Inorganic Salt Clusters to Antibody Conjugates and Beyond

Campuzano

Nshanian

Spahr

et al. 2020

J. Am. Soc. Mass Spectrom.

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Analysis of proteins and complexes under native mass spectrometric (MS) and solution conditions was typically performed using time-of-flight (ToF) analyzers, due to their routine high m/z transmission and detection capabilities. However, over recent years, the ability of Orbitrap-based mass spectrometers to transmit and detect a range of high molecular weight species is well documented. Herein, we describe how a 15 Tesla Fourier transform ion cyclotron resonance mass spectrometer (15 T FT-ICR MS) is more than capable of analyzing a wide range of ions in the high m/z scale (>5000), in both positive and negative instrument polarities, ranging from the inorganic cesium iodide salt clusters; a humanized IgG1k monoclonal antibody (mAb; 148.2 kDa); an IgG1-mertansine drug conjugate (148.5 kDa, drug-toantibody ratio; DAR 2.26); an IgG1-siRNA conjugate (159.1 kDa; ribonucleic acid to antibody ratio; RAR 1); the membrane protein aquaporin-Z (97.2 kDa) liberated from a C8E4 detergent micelle; the empty MSP1D1-nanodisc (142.5 kDa) and the tetradecameric chaperone protein complex GroEL (806.2 kDa; GroEL dimer at 1.6 MDa). We also investigate different regions of the FT-ICR MS that impact ion transmission and desolvation. Finally, we demonstrate how the transmission of these species and resultant spectra are highly consistent with those previously generated on both quadrupole-ToF (Q-ToF) and Orbitrap instrumentation. This report serves as an impactful example of how FT-ICR mass analyzers are competitive to Q-ToFs and Orbitraps for high mass detection at high m/z.

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Section: Resultssupporting

confidence: 92%

Section: ■ Results and Discussionmentioning

confidence: 68%

High Mass Analysis with a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: From Inorganic Salt Clusters to Antibody Conjugates and Beyond

Campuzano

Nshanian

Spahr

et al. 2020

J. Am. Soc. Mass Spectrom.

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“…14 The key strengths of the ICR and FT-ICR methods in the study of negative metal ion chemistry are (1) complex reaction sequences can be sorted out with double-resonance ejection procedures for isolating a reactive ion or establishing a reactant ion/product ion connection; (2) pulsed-valve reagent inlets can permit the study of metal ion reactions in the absence of potentially reactive neutral precursors; (3) a variety of ion source configurations may be employed, including solid probes and laser desorption;15 (4) the low pressure in the system permits direct use of relatively involatile metal compounds; and (5) quite high resolution and high mass ranges may be achieved. 16 ICR-based methods are not without certain disadvantages. Because of the low pressure in the reaction cell, there is uncertainty regarding the energy distribution of the trapped ions.…”

Section: A Ion Cyclotron Resonancementioning

confidence: 99%

Gas-Phase transition-metal negative ion chemistry

Squires¹

1987

Chem. Rev.

119

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“…Due to its high resolving power, mass accuracy, and ability to be coupled with versatile fragmentation techniques, FTICR MS has long been recognized for its top-down capabilities for direct protein sequencing, characterization of PTMs, and probing protein-ligand interactions. 18 – 21 Although the detection of molecules of high mass-to-charge ( m/z up to 16,241) using FTICR was demonstrated three decades ago 22 , its capability to transmit and analyze macromolecular protein complexes has yet to be demonstrated. The previous FTICR record of identifying a 669 kDa thyroglobulin dimer was achieved by recording its fragment ions rather than its intact dimer or denatured form, leaving the transmission and detection ability of FTICR for large complexes still in question 23 .…”

mentioning

confidence: 99%

An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes

et al. 2018

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Mass spectrometry (MS) has become a crucial technique for the analysis of protein complexes. Native MS has traditionally examined protein subunit arrangements, while proteomics MS has focused on sequence identification. These two techniques are usually performed separately without harvesting the synergies between them. Here we describe the development of an integrated native MS and top-down proteomics method using Fourier transform ion cyclotron resonance (FTICR) to analyze macromolecular protein complexes in a single experiment. We address previous concerns of employing FTICR MS to measure large macromolecular complexes by demonstrating the detection of complexes up to 1.8 MDa, and we demonstrate the efficacy of this technique for direct acquirement of sequence to higher order structural information with several large complexes. We then summarize the unique functionalities of different activation/dissociation techniques. The platform expands the ability of MS to integrate proteomics and structural biology to provide insights into protein structure, function and regulation.

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Detection of mass 16241 ions by Fourier-transform mass spectrometry

Cited by 41 publications

References 34 publications

High Mass Analysis with a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: From Inorganic Salt Clusters to Antibody Conjugates and Beyond

High Mass Analysis with a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: From Inorganic Salt Clusters to Antibody Conjugates and Beyond

Gas-Phase transition-metal negative ion chemistry

An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes

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