Tutorial: Ion Activation in Tandem Mass Spectrometry Using Ultra‐high Resolution Instrumentation

Bayat, Parisa; Lesage, Denis; Cole, Richard B.

doi:10.1002/mas.21623

Cited by 34 publications

(47 citation statements)

References 179 publications

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“…HCD-induced fragmentation can improve the yield of low molecular weight fragment ions carrying important structural information due to the multiple collisions of precursor ions and fragments ions with gas molecules [38]. Moreover, HCD is a higher energy alternative to CID, and therefore a lower NCE is required to achieve the same degree of fragmentation [19,39]. This may be why it is still possible to detect the typical NL of HNO 2 using a lower NCE.…”

Section: Discussionmentioning

confidence: 99%

Advancing Target Identification of Nitrated Phospholipids in Biological Systems by HCD Specific Fragmentation Fingerprinting in Orbitrap Platforms

et al. 2020

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Nitrated phospholipids have recently been detected in vitro and in vivo and associated with beneficial health effects. They were identified and quantified in biological samples by lipidomics methodologies using liquid chromatography-collision-induced dissociation (CID) tandem mass spectrometry (MS/MS) acquired with the linear ion trap mass spectrometer. Only a few studies have used higher-energy collision dissociation (HCD)-MS/MS in high-resolution Orbitraps to characterize nitrated phosphatidylserines and nitrated cardiolipins, highlighting the marked differences in the fragmentation patterns when using CID or HCD fragmentation methods. In this study, we aimed to evaluate the fragmentation of nitrated phosphatidylcholine and nitrated phosphatidylethanolamine species under HCD-MS/MS. We studied the effect of normalized collision energy (NCE) in the fragmentation pattern to identify the best acquisition conditions and reporter ions to detect nitrated phospholipids. The results showed that the intensity of the typical neutral loss of nitrous acid (HNO2) diminishes with increasing NCE, becoming non-detectable for a higher NCE. Thus, the loss of HNO2 could not be the most suitable ion/fragment for the characterization of nitrated phospholipids under HCD. In HCD-MS/MS new fragment ions were identified, corresponding to the nitrated fatty acyl chains, NO2-RCOO−, (NO2-RCOOH-H2O + H)+, and (NO2-RCOOH + H)+, suggested as potential reporter ions to detect nitrated phospholipids when using the HCD-MS/MS lipidomics analysis.

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Section: Discussionmentioning

confidence: 99%

Advancing Target Identification of Nitrated Phospholipids in Biological Systems by HCD Specific Fragmentation Fingerprinting in Orbitrap Platforms

et al. 2020

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“…Early activation methods explored in MS/MS focused on increasing the internal energy of ions by energetic collisions with neutral collision gas particles. Collisional activation of ions can be achieved in a variety of mass spectrometers, including quadrupole, time‐of‐flight, or ion cyclotron resonance (ICR) mass analyzers 3,4 . Until now, tandem mass spectrometry with collision‐induced dissociation (CID) remains a widely used approach to produce fragment ions of peptides to identify proteins in the field of proteomics 3 …”

Section: Introductionmentioning

confidence: 99%

“…3,4 Until now, tandem mass spectrometry with collisioninduced dissociation (CID) remains a widely used approach to produce fragment ions of peptides to identify proteins in the field of proteomics. 3 Collisional activation, however, is less efficient for sequence analysis of large biological ions, such as intact proteins or protein complexes. Top-down sequence and structure analysis of intact proteins and protein complexes is often more efficiently accomplished by alternative activation methods, such as surface-induced dissociation, 5 electron-based dissociation (electron transfer/capture dissociation), 6,7 or ultraviolet photodissociation (UVPD).…”

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confidence: 99%

Tandem‐trapped ion mobility spectrometry/mass spectrometry coupled with ultraviolet photodissociation

Liu

Ridgeway

Winfred

et al. 2021

Rapid Comm Mass Spectrometry

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Rationale Tandem‐ion mobility spectrometry/mass spectrometry methods have recently gained traction for the structural characterization of proteins and protein complexes. However, ion activation techniques currently coupled with tandem‐ion mobility spectrometry/mass spectrometry methods are limited in their ability to characterize structures of proteins and protein complexes. Methods Here, we describe the coupling of the separation capabilities of tandem‐trapped ion mobility spectrometry/mass spectrometry (tTIMS/MS) with the dissociation capabilities of ultraviolet photodissociation (UVPD) for protein structure analysis. Results We establish the feasibility of dissociating intact proteins by UV irradiation at 213 nm between the two TIMS devices in tTIMS/MS and at pressure conditions compatible with ion mobility spectrometry (2–3 mbar). We validate that the fragments produced by UVPD under these conditions result from a radical‐based mechanism in accordance with prior literature on UVPD. The data suggest stabilization of fragment ions produced from UVPD by collisional cooling due to the elevated pressures used here (“UVnoD2”), which otherwise do not survive to detection. The data account for a sequence coverage for the protein ubiquitin comparable to recent reports, demonstrating the analytical utility of our instrument in mobility‐separating fragment ions produced from UVPD. Conclusions The data demonstrate that UVPD carried out at elevated pressures of 2–3 mbar yields extensive fragment ions rich in information about the protein and that their exhaustive analysis requires IMS separation post‐UVPD. Therefore, because UVPD and tTIMS/MS each have been shown to be valuable techniques on their own merit in proteomics, our contribution here underscores the potential of combining tTIMS/MS with UVPD for structural proteomics.

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“…The complete lack of signals could only be explained by either of the two possibilities that the IR laser also activated formed fragment ions and as a result these further decomposed. During low energy CID in the linear ion trap (LIT), the energy is mostly transferred to the precursor ions and resulting fragments are less activated 41,42 . In case of IRMPD, Al‐EDTA fragmentation might have resulted in formation of mostly [Al] x+ ions or other small fragment ions that lay outside the possible mass range (m/z 50–500).…”

Section: Resultsmentioning

confidence: 99%

Fragmentation behavior of EDTA complexes under different activation conditions

Beck

2021

J Mass Spectrom

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Ethylenediaminetetraacetic acid (EDTA) is an aminopolycarboxylic acid and complexation agent that is able to bind a large variety of metals. The formation of highly stable metal‐EDTA complexes is generally very quick. This has led to the use of EDTA in a variety of applications, including food, medical, and household applications. In the current study, we have investigated the fragmentation behavior of EDTA and various metal complexes under collision‐induced dissociation (CID), infrared‐multiphoton dissociation (IRMPD), and higher‐energy collisional dissociation (HCD) activation conditions. Both, positive and negative mode electrospray ionization (ESI) were applied. The metals used to complex with EDTA ranged from alkaline earth metals, such as sodium and cesium, via calcium, nickel, zinc, aluminum, copper, iron, and indium to yttrium and several lanthanides. Furthermore, the protonated and deprotonated species of EDTA, as well as disodium and trisodium species, have been subjected to fragmentation. The results show that characteristic fragmentations were obtained for EDTA and the metal complexes under the investigated conditions. The use of an ion cyclotron resonance (ICR) and an Orbitrap mass spectrometer, as high resolution‐accurate mass instruments, allowed the assignment of elemental compositions undoubtedly for the vast majority of fragments. Certain trends were observed that trend correlated with the size of the metal and the location within the periodic table.

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Tutorial: Ion Activation in Tandem Mass Spectrometry Using Ultra‐high Resolution Instrumentation

Cited by 34 publications

References 179 publications

Advancing Target Identification of Nitrated Phospholipids in Biological Systems by HCD Specific Fragmentation Fingerprinting in Orbitrap Platforms

Advancing Target Identification of Nitrated Phospholipids in Biological Systems by HCD Specific Fragmentation Fingerprinting in Orbitrap Platforms

Tandem‐trapped ion mobility spectrometry/mass spectrometry coupled with ultraviolet photodissociation

Fragmentation behavior of EDTA complexes under different activation conditions

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