Ion Trap Mass Analyzer Research Articles

Considerations for Generating Frequency Modulation Waveforms for Fourier Transform-Ion Mobility Experiments.

By casting the information regarding an ion population's mobility in the frequency domain, the coupling of time-dispersive ion mobility techniques is now imminently compatible with slower mass analyzers such as ion traps. Recent reports have detailed the continued progress toward maximizing the efficiency of the Fourier transform ion mobility-mass spectrometry (FT-IM-MS) experiments, but few reports have outlined the intersection between the practical considerations of implementation against the theoretical limits imposed by traditional signal processing techniques. One of the important concerns for Fourier-based multiplexing experiments is avoiding signal aliasing as a product of undersampled signals that may occur during data acquisition. In addition to traditional considerations such as detector sampling frequency, the limitations (i.e., maximum measurable drift time) imposed by experimental mass scan duration and the frequency sweep used for ion gate modulation must also be assessed. This work aims to connect the fundamental underpinnings of FT-IM-MS experiments and the associated experimental parameters that are encountered when coupling the comparatively fast separations in the mobility domain with the slower m/z scanning common for ion-trap mass analyzers. In addition to stating the relevant theory that applies to the FT-IM-MS experiment, this report highlights how aliased signals will manifest post Fourier transform in reconstructed arrival time distributions and calculated mobilities.

Abstract 3916: Cyanobacterial natural product Sec61α inhibitors induce broad suppression of the glioma cell secretome

Abstract Coibamide A is a cyclopeptide natural product with potent antiproliferative activity against cultured human cancer cells and subcutaneous U87-MG glioblastoma tumors in mice. We have recently determined that coibamide A binds to the Sec61 translocon channel at a site that is close, but not identical, to the binding site of the peptide/polyketide natural product apratoxin A. As the majority of secreted proteins in mammalian cells are trafficked through the conventional secretory pathway via the Sec61 translocon, this raised the possibility that coibamide A and apratoxin A block import and secretion of different Sec61 client proteins. In the present study, we analyzed and compared the secretome of human U87-MG glioblastoma cells in the presence and absence of both marine natural products. U87-MG glioblastoma cells were treated with coibamide A (5 nM), apratoxin A (5 nM), or vehicle for 24 h. The growth media was then replaced with serum-free media for a further 24 h. Tryptic proteomic samples were generated from cell-free conditioned media and analyzed on a LC-coupled Orbitrap Fusion mass spectrometer. The high-resolution Orbitrap mass analyzer was used to both identify precursor ions for tandem mass (MS2) analysis in the ion trap mass analyzer and to quantitate those ions (MS1). Secreted proteins were identified from peptide–spectrum matches to the human protein database using a decoy database to assign an FDR and quantified from their MS1 ion intensities. Comparison of mass spectrometric data against the human secretome database revealed 175 proteins in the U87-MG cell secretome that were identified with high confidence. Differences between coibamide A and apratoxin A treatment were not significant, however both Sec61 inhibitors induced significant suppression of the U87-MG secretome relative to vehicle-treated cells. Treatment with coibamide A or apratoxin A resulted in the reduction of 75% of quantifiable secretome (131 proteins). Of the remaining 44 proteins, 34 are directed to intracellular organelles or contain a motif associated with retention in the endoplasmic reticulum and 10 were not suppressed with treatment but were hypothesized to be Sec61 clients. Malignant glioblastoma cells secrete proteins into the extracellular space and use complex intercellular signaling mechanisms for a survival advantage. Our results indicate that broad-acting inhibitors of Sec61-dependent co-translational translocation block the progression of a significant percentage of the U87-MG glioblastoma cell secretome including several proteins that have previously been detected as biomarkers in the cerebrospinal fluid, blood, or urine of brain tumor patients. Taken together, our work illustrates the feasibility of inducing a reversible suppression of numerous (undrugged) extracellular signals by targeting Sec61-dependent protein biogenesis in the secretory pathway with drug-like molecules. Citation Format: Daphne R. Mattos, Jeffrey D. Serrill, Philip R. Gafken, Kerry L. McPhail, Walter K. Vogel, Jane E. Ishmael. Cyanobacterial natural product Sec61α inhibitors induce broad suppression of the glioma cell secretome [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 3916.

Prosit-TMT: Deep Learning Boosts Identification of TMT-Labeled Peptides.

The prediction of fragment ion intensities and retention time of peptides has gained significant attention over the past few years. However, the progress shown in the accurate prediction of such properties focused primarily on unlabeled peptides. Tandem mass tags (TMT) are chemical peptide labels that are coupled to free amine groups usually after protein digestion to enable the multiplexed analysis of multiple samples in bottom-up mass spectrometry. It is a standard workflow in proteomics ranging from single-cell to high-throughput proteomics. Particularly for TMT, increasing the number of confidently identified spectra is highly desirable as it provides identification and quantification information with every spectrum. Here, we report on the generation of an extensive resource of synthetic TMT-labeled peptides as part of the ProteomeTools project and present the extension of the deep learning model Prosit to accurately predict the retention time and fragment ion intensities of TMT-labeled peptides with high accuracy. Prosit-TMT supports CID and HCD fragmentation and ion trap and Orbitrap mass analyzers in a single model. Reanalysis of published TMT data sets show that this single model extracts substantial additional information. Applying Prosit-TMT, we discovered that the expression of many proteins in human breast milk follows a distinct daily cycle which may prime the newborn for nutritional or environmental cues.

Synchronized Stepped Frequency Modulation for Multiplexed Ion Mobility Measurements.

Implementation of frequency-encoded multiplexing for ion mobility spectrometry (e.g., Fourier transform ion mobility spectrometry (FT-IMS)) has facilitated the direct coupling of drift tube ion mobility instrumentation with ion-trap mass analyzers despite their duty cycle mismatch. Traditionally, FT-IMS experiments have been carried out to utilize continuous linear frequency sweeps that are independent of the scan rate of the ion-trap mass analyzer, thus creating a situation where multiple frequencies are swept over two sequential mass scans. This in turn creates a degree of ambiguity in which the ion current derived from a single modulation frequency cannot be assigned to a single data point in the frequency-modulated signal. In an effort to eliminate this ambiguity, this work describes a discrete stepwise function to modulate the ion gates of the IMS while synchronization between the generated frequencies and the scan rate of the linear ion trap is achieved. While the number of individual frequencies used in the stepped frequency sweeps is less than in continuous linear modulation experiments, there is no loss in performance and high levels of precision are maintained across differing combinations of terminal frequencies and scan lengths. Furthermore, the frequency-scan synchronization enables further data-processing techniques such as linear averaging of the frequency modulated signal to drastically improve signal-to-noise ratio for both high and low intensity analytes.

Enabling point-of-need chemical detection by miniaturizing ion-trap mass spectrometry

There exists a wide-ranging need to provide both qualitative and quantitative chemical information in near-real time outside of the laboratory environment. In response to this need, efforts in recent years have focused on the transition of laboratory-based instruments for chemical analysis into field-portable forms. Of the many techniques for chemical analysis, mass spectrometry has been an active area for miniaturization efforts due to the quality of chemical information the technique can provide and its ability to operate either stand-alone or coupled with additional analytical techniques. In this mini-review, we provide an overview of what we term ‘point-of-need’ chemical measurements and summarize the various means by which they can be generated. We then transition to focus exclusively on the application of mass spectrometry and specifically on the miniaturization of ion-trap mass analyzers to enable this class of measurements. Examples are provided that demonstrate how this technology has been developed and used within the point-of-need application space.

Genetic algorithm parallel optimization of a new high mass resolution planar electrostatic ion trap mass analyzer.

The study and design of high-resolution mass analyzers is a very important task in mass spectrometry. A planar electrostatic ion trap (PEIT) mass analyzer with image charge detection and FT-based data processing has been developed, theoretically simulated, and experimentally validated. However, the 10 ring electrode configuration (PEIT-10) is difficult for mechanical construction and voltage tuning; moreover, few methods have been reported for optimizing the performance of multi-electrode mass analyzers. In this article, a simplified PEIT-7 mass analyzer was designed, and a genetic algorithm parallel optimization (GAPO) method was developed for optimizing multiple voltage settings of the new PEIT-7 mass analyzer to achieve spatial and energy isochronicity as well as iso-coordinate property. The automatic voltage optimization processes for the reduction of time aberration and spatial aberration showed that the developed GAPO method can significantly improve the optimization efficiency (the optimal voltage set being found within 5 hours with a maximum time aberration of 15 ps and a maximum z aberration of 0.10 μm). Based on the results obtained from the GAPO method, the resolving power of the PEIT-7 mass analyzer for six groups of ions with closely packed masses (m/z = 117.000 Th to 117.010 Th) was demonstrated, and a mass resolution of 171k was achieved at an acquisition time of 200 ms. The established GAPO method facilitates the design and optimization of high-resolution mass analyzers and may be useful for the design of other multi-electrode ion optical devices.

Liquid Chromatography-Tandem Mass Spectrometry-Based Profiling of Plant Hormones.

Phytohormones plays crucial physiological functions in plants, where they are involved in plant development, reproduction, defense, and many other functions. Phytohormones production has been found to be regulated in response to abiotic and biotic factors affecting the plant metabolism, and therefore, biosynthesis of primary and secondary metabolites. Thus, the detection and quantification of phytohormones in different plant tissues are essential to be determined unraveling the various plant metabolic pathways and behavior. Yet phytohormones analysis is always problematic, since they are found in extremely low concentrations and have a wide range of chemical and physicochemical properties. As a result, the ideal method should start with an appropriate extraction procedure followed by quantification by highly sensitive instrumental techniques providing precise and robust results. The current chapter presents an improved extraction method based on liquid-liquid extraction from a 50-mg aliquot of plant tissue for analysis of the major classes of phytohormones. Then, mass spectrometry (MS) analysis is conducted using quadrupole/linear ion trap (QLIT) mass analyzer equipped with electrospray ionization (ESI) source after a liquid chromatographic separation step. The developed method demonstrates an appropriate feasibility addressing biological questions related to phytohormones production and regulation.

Two-Dimensional Partial Covariance Mass Spectrometry for the Top-Down Analysis of Intact Proteins.

Two-dimensional partial covariance mass spectrometry (2D-PC-MS) exploits the inherent fluctuations of fragment ion abundances across a series of tandem mass spectra, to identify correlated pairs of fragment ions produced along the same fragmentation pathway of the same parent (e.g., peptide) ion. Here, we apply 2D-PC-MS to the analysis of intact protein ions in a standard linear ion trap mass analyzer, using the fact that the fragment-fragment correlation signals are much more specific to the biomolecular sequence than one-dimensional (1D) tandem mass spectrometry (MS/MS) signals at the same mass accuracy and resolution. We show that from the distribution of signals on a 2D-PC-MS map it is possible to extract the charge state of both parent and fragment ions without resolving the isotopic envelope. Furthermore, the 2D map of fragment-fragment correlations naturally separates the products of the primary decomposition pathways of the molecular ions from those of the secondary ones. We access this spectral information using an adapted version of the Hough transform. We demonstrate the successful identification of highly charged, intact protein molecules bypassing the need for high mass resolution. Using this technique, we also perform the in silico deconvolution of the overlapping fragment ion signals from two co-isolated and co-fragmented intact proteins, demonstrating a viable new method for the concurrent mass spectrometric identification of a mixture of intact protein ions from the same fragment ion spectrum.

Eco-Friendly Pharmaceutical Analysis of Rifaximin in Tablets by HPLC-MS and Microbiological Turbidimetry.

Rifaximin, an antimicrobial used for the treatment of various diseases, lacks analytical methods in official compendia for evaluation of the final product. This paper presents an eco-friendly protocol for rifaximin tablets by high performance liquid chromatography coupled with mass spectrometry (HPLC-MS). The method was completely validated according to the International Conference on Harmonization guidelines and developed following the concept of Quality by Design. The separation was achieved using a C18 column, purified water +0.1% glacial acetic acid and ethyl alcohol, 52:48 (v/v), as mobile phase, 0.9mLmin-1 at 290nm and ambient room temperature. Mass spectral analyses were performed using electrospray ionization (ESI) ion source and ion trap mass analyzer. The method was linear over the concentration range of 5-50μgmL-1. The sample was subjected to acidic, basic, neutral, oxidative and photolytic degradation. Degradation products did not interfere in the quantification of the rifaximin, so the method can be considered indicative of stability. Degradation products were also evaluated individually by microbiological method using Escherichia coli. The validated method could be used promisingly as green analytical strategies for detection and quantification of rifaximin in tablets.

Protein Analysis by Electrospray-Orbital Frequency Analyzer with Charge Detection Mass Spectrometry Algorithm.

Orbital frequency analyzer (OFA) is one of the electrostatic ion trap mass analysers for FTMS, which offers ultrahigh mass resolution and high ion charge capacity. In order to analyze multiply charged proteins and other large biological particles by means of charge detection mass spectrometry, a data processing algorithm was created to suit the image charge signal of nonharmonic waveform nature. The algorithm is capable of detecting collisions between ions and residual gas molecules, to determine lifetime of ions, and to evaluate the charge and mass values for ions having lifetime above a threshold. With the filtering of the lifetime and charge value, the chemical noise from small molecules and protein fragments can be eliminated in the reconstructed spectrum, facilitating measurement of protein content at a very low concentration, down to tens of nanomolars. The standard deviation of charge measurement is between 1.1 to 1.8 e for ions with oscillation lifetimes from 1 to 0.4 s, and this in turn determines the CDMS spectrum mass peak width. It has been found that the lower voltage setting of the OFA results in a larger population of ions surviving for longer times and thus produces narrower mass peak width. While OFA is able to run multiplexed CDMS without ion motion interference, coexisting ions of the same or very close m/z can cause interference between their image charge signals, which increases the error in charge determination.

Investigation of the effect of an octopole electric field on a linear ion trap and an asymmetric semi-circular linear ion trap analyzer.

Linear ion trap mass analyzer could improve analytical performance compared to the traditional three-dimensional ion trap. In this study, a systematic investigation of the effect of octopole field on the performance of linear quadrupole ion trap was studied by both theoretical simulations and experiments. An asymmetric semi-circular linear ion trap (AsC-LIT) analyzer was designed and tested based on the theoretical results. The AsC-LIT consists of one pair of larger semi-circular rods with radius Ry and one pair of smaller semi-circular rods with radius Rx (Ry > Rx) in the cross section for introducing the quantitative octopole field. The analytical performances of these simplified AsC-LITs with different amounts of octopole fields were carefully investigated using both theoretical simulations and experimental validation. Experimental results showed that it could have a mass resolution of 1645 at m/z 175 (arginine); furthermore, the low mass cutoff and CID efficiency can be significantly improved when some positive octopole is added. The simulative results indicated that 2.56% octopole component was the best choice for achieving higher analytical performances. The theoretical and experimental studies of this work could certainly enrich the knowledge of a higher order electric field effect on the linear ion trap, furthermore, the simple geometric design and performance characteristics of this new AsC-LIT make it particularly attractive in the development of miniaturized mass spectrometers.

Digital ion trap mass analysis of high mass protein complexes using IR activation coupled with ion/ion reactions

Native mass spectrometry (MS) focuses on measuring the masses of large biomolecular complexes and probing their structures. Large biomolecular complexes are readily introduced into mass spectrometers as gas-phase ions using electrospray ionization (ESI); however, the ions tend to be heavily adducted with solvent and salts, which leads to mass measurement errors. Various solution clean-up approaches can reduce the degree of adduction prior to introduction to the mass spectrometer. Gas-phase activation of trapped ions can provide additional adduct reduction, and charge reduction ion/ion reactions increase charge state separation. Together, gas-phase activation and charge reduction can combine to yield spectra of well separated charge states for improved mass measurements. A simple gas-phase collisional activation technique is to apply a dipolar DC (DDC) field to opposing electrodes in an ion trap. DDC activation loses its efficacy when ions are trapped at low q values, which is true of the high m/z ions generated by charge reduction ion/ion reactions. Digital ion trapping (DIT) readily traps high m/z ions at higher q values by varying trapping frequency rather than amplitude, but the low frequencies used to trap high m/z ions also decreases the efficacy of DDC activation. We demonstrate here using ions derived from GroEL that IR activation of ions shows no discrimination against high m/z ions trapped with DIT, because they can be focused equally well to the trap center to interact with the IR laser beam. Following pump out of excess background gas, IR activation can also induce efficient dissociation of the GroEL complex. This work demonstrates that IR activation is an effective approach for ion heating in native MS over the unusually wide range of charge states accessible via gas-phase ion/ion reactions.

Drug screening by using the Toxtyper™ LC-ion trap MS: Optimization of its application on serum samples in a DUID context

The toxicological approach for monitoring Driving Under Influence of Drugs (DUID) requires analytical techniques with a broad spectrum of identification coupled to a high analytical sensitivity. In this context immunological methods are generally used, while GC or LC-MS are applied for the confirmation step. A different approach for drug screening is represented by the Toxtyper™ instrumentation, an LC-MS platform equipped with a high-speed ion trap mass analyzer, provided with ready-to-use protocols and a database of as many as 4500 therapeutic, toxic/illicit drugs and metabolites. The aim of the present work was to verify its performances in real conditions of drug screening of human serum in the context of DUID. To test and compare its analytical performances, four pooled serum samples were fortified with a selected panel of 47 drugs and metabolites. The agreement between the results from the ToxtyperTM and from the confirmatory techniques currently in use at the University of Verona (GC and LC-MS) was investigated by analyzing 90 real samples chosen from those routinely analyzed. The present study highlights the suitability of the ToxtyperTM for drug screening in serum with a sensitivity compatible with the needs of the DUID for all the tested compounds, with the only exception of cannabinoids.

Enabling Isotope Ratio Measurements on an Ion Trap Mass Spectrometer.

For portable, remotely operated systems in space and defense, relaxed vacuum requirements are a strong advantage of ion trap mass analyzers. However, ion traps are believed to have insufficient capability for isotope ratio measurement because they fundamentally restrict sampling capacity. Focusing on modifications to the detection sequence of a digitally driven 3D quadrupole ion trap, operating in resonance ejection mode, we investigated improved performance for isotope ratio precision and accuracy. Due to xenon's inert nature and wide span of isotopes, xenon isotope ratios provide an excellent marker of processes (e.g. radioactive decay and planetary atmospheric escape) which would be ideally measured by in situ mass spectrometry. To target xenon isotope ratio analysis specifically, we implemented data acquisition system modifications for enhanced y-axis resolution measurements and signal filtering. In this manner, we show measurement precision improvements from ~±100 0/00 to ~±0.1 0/00 and accuracy improvements from ~30 0/00 to ~0.5 0/00 for our targeted isotopes of interest.

Field analyses of lavender volatile organic compounds: performance evaluation of a portable gas chromatography–mass spectrometry device

In situ analysis of volatile organic compounds (VOCs) emitted by plants is an important challenge in chemical ecology. The traditional approach usually consists in trapping compounds using dynamic headspace extraction (DHS) in-field, followed by gas chromatography analysis coupled with mass spectrometry (GC-MS and/or GC-FID) in the laboratory. In this study, we evaluated the use of the new portable Torion T-9 GC-MS system for rapid and in situ analysis of VOCs emitted by fine lavender and lavandin species. All field analyses were performed using a person-portable low-thermal mass GC system coupled with a miniature toroidal ion trap mass analyser (ppGC-ITMS): Torion T-9 portable GC-MS. Subsequently, multivariate statistical analyses were performed to determine chemical differences between species. Thirty compounds were separated and detected in all lavender above-ground samples in only 3 min of analysis. The portable GC-MS device enabled a rapid in-field distinction of Lavandula species based on their detected volatile profiles.

RHOA and mDia1 Promotes Apoptosis of Breast Cancer Cells Via a High Dose of Doxorubicin Treatment.

BackgroundTransforming RhoA proteins (RHOA) and their downstream Diaphanous homolog 1 proteins (DIAPH1) or mDia1 participate in the regulation of actin cytoskeleton which plays critical role in cells, i.e., morphologic changes and apoptosis.MethodologyTo determine the cell viability the real time cell analysis (RTCA) and flow cytometry were used. To perform proteomic analysis, the label-free quantitative method and post-translation modification by the nano-HPLC and ESI-MS ion trap mass analyser were used.ResultsThe results of the cell viability showed an increase of dead cells (around 30 %) in MCF-7/DOX-1 (i.e., 1μM of doxorubicin was added to MCF-7/WT breast cancer cell line) compared to MCF-7/WT (control) after 24 h doxorubicin (DOX) treatment. The signalling pathway of the Regulation of actin cytoskeleton (p<0.0026) was determined, where RHOA and mDia1 proteins were up-regulated. Also, post-translational modification analysis of these proteins in MCF-7/DOX-1 cells revealed dysregulation of the actin cytoskeleton, specifically the collapse of actin stress fibbers due to phosphorylation of RHOA at serine 188 and mDia1 at serine 22, resulting in their deactivation and cell apoptosis.ConclusionThese results pointed to an assumed role of DOX to dysregulation of actin cytoskeleton and cell death.

Applications of Infrared Multiple Photon Dissociation (IRMPD) to the Detection of Posttranslational Modifications.

Infrared multiple photon dissociation (IRMPD) spectroscopy allows for the derivation of the vibrational fingerprint of molecular ions under tandem mass spectrometry (MS/MS) conditions. It provides insight into the nature and localization of posttranslational modifications (PTMs) affecting single amino acids and peptides. IRMPD spectroscopy, which takes advantage of the high sensitivity and resolution of MS/MS, relies on a wavelength specific fragmentation process occurring on resonance with an IR active vibrational mode of the sampled species and is well suited to reveal the presence of a PTM and its impact in the molecular environment. IRMPD spectroscopy is clearly not a proteomics tool. It is rather a valuable source of information for fixed wavelength IRMPD exploited in dissociation protocols of peptides and proteins. Indeed, from the large variety of model PTM containing amino acids and peptides which have been characterized by IRMPD spectroscopy, specific signatures of PTMs such as phosphorylation or sulfonation can be derived. High throughput workflows relying on the selective fragmentation of modified peptides within a complex mixture have thus been proposed. Sequential fragmentations can be observed upon IR activation, which do not only give rise to rich fragmentation patterns but also overcome low mass cutoff limitations in ion trap mass analyzers. Laser-based vibrational spectroscopy of mass-selected ions holding various PTMs is an increasingly expanding field both in the variety of chemical issues coped with and in the technological advancements and implementations.

Ambient Lipidomic Analysis of Single Mammalian Oocytes and Preimplantation Embryos Using Desorption Electrospray Ionization (DESI) Mass Spectrometry.

Desorption electrospray ionization (DESI) is a spray-based ambient ionization method for mass spectrometry (MS) that generates ions in native atmospheric conditions (e.g., pressure and temperature). Ambient ionization allows in situ analysis of unmodified samples by eliminating analyte extraction and separation steps before MS. Lipid analysis of individual mammalian oocytes and preimplantation embryos is challenging because of their complex chemical composition and minute dimensions (100-300μm in diameter). Nonetheless, DESI-MS can provide comprehensive lipidomic profiles of individual oocytes or embryos using a fast and simple workflow. DESI-MS lipid profiles include many classes of lipids such as phosphatidylcholines (PC), triacylglycerols (TAG), free fatty acids (FFA), phosphatidylethanolamines (PE), phosphatidylinositols (PI), phosphatidylserines (PS), diacylglycerols (DAG), ubiquinone, cholesterol and cholesterol derivatives (e.g., cholesterol sulfate and cholesterol esters). Depending on the mass spectrometer used, there is the additional possibility of obtaining structural information of lipids via MSn, and molecular formulae via high resolution MS. Here, we describe the procedures for sample handling, the DESI-MS experimental arrangement, and the data collection and data analysis using low and high-resolution mass spectrometers (such as a linear ion trap and Orbitrap mass analyzer, respectively), as well as strategies for structural characterization of lipids. Lastly, we detail our workflow for relating the chemical information obtained by DESI-MS into the biological context of oocyte and embryo metabolism.

Pseudo-Multiple Reaction Monitoring (Pseudo-MRM) Mode on the "Brick" Mass Spectrometer, Using the Grid-SWIFT Waveform.

Besides portability and increasingly improved performances, the ability of screening target analyte from complex compounds is a crucial function of miniature mass spectrometers, especially for in situ analysis. Selected reaction monitoring (SRM) and multiple reaction monitoring (MRM) operation modes are the most widely used mass spectrometry operation methods for target analyte quantitation. As a continuous effort to improve the analytical performances of the "brick" mass spectrometer, built in-house, pseudo-SRM and pseudo-MRM modes were realized on the linear ion trap mass analyzer in the device. A broadband excitation waveform in both time and frequency domains, namely, the Grid-SWIFT waveform, was constructed and compared with the conventional SWIFT waveform. By isolating target ions during the ion introduction period using the Grid-SWIFT waveform, target ions could be efficiently accumulated inside the ion trap without experiencing space charge effects and interferences from nontarget ions in the samples. As a result, not only the detection sensitivity of the target analyte could be increased, but also the quantitation accuracy over a relatively wide concentration range could be improved.

Tailoring fields of one-sheet and two-sheet planar ion trap mass analyzers

In this paper, a simulation study on tailoring the fields in planar ion trap geometries for making them suitable for mass analysis is presented. Two different planar trap geometries were considered: the first is a One-Sheet Ion Trap Geometry in which the ions are trapped off-plane and the second is a Two-Sheet Ion Trap Geometry in which the ions are trapped in between the two sheets. Both DC and RF potentials were used to trap ions.The fields were tailored to obtain linear trapping fields in these two geometries. This was done by splitting the central electrode into segments and applying suitable DC potentials to them. The potentials were computed using a least square method. The simulations were carried out considering a printed circuit board (PCB) with a Teflon base. The One-Sheet Ion Trap Geometry consists of five electrodes, of which the central electrode is segmented. In Two-Sheet Ion Trap Geometry, each sheet consists of three electrodes, of which the central electrode is segmented.The method outlined in the study is able to tailor fields to be linear as well as mildly superlinear.