Browse
Submit Data
Databases
API
Help

Dataset Information

17 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Ultra-Fast Polarity Switching, Non-Radioactive Drift Tube for the Miniaturization of Drift-Time Ion Mobility Spectrometer.

ABSTRACT: Drift-time ion mobility spectrometer (DT-IMS) is a promising technology for gas detection and analysis in the form of miniaturized instrument. Analytes may exist in the form of positively or negatively charged ions according to their chemical composition and ionization condition, and therefore require both polarity of electric field for the detection. In this work the polarity switching of a drift-time ion mobility spectrometer based on a direct current (DC) corona discharge ionization source was investigated, with novel solutions for both the control of ion shutter and the stabilization of aperture grid. The drift field is established by employing a switchable high voltage power supply and a serial of voltage regulator diode, with optocouplers to drive the ion shutter when the polarity is switched. The potential of aperture grid is stabilized during the polarity switching by the use of four diodes to avoid unnecessary charging cycle of the aperture grid capacitor. Based on the proposed techniques, the developed DT-IMS with 50 mm drift path is able to switch its polarity in 10 ms and acquire mobility spectrum after 10 ms of stabilization. Coupled with a thermal desorption sampler, limit of detection (LoD) of 0.1 ng was achieved for ketamine and TNT. Extra benefits include single calibration substance for both polarities and largely simplified pneumatic design, together with the reduction of second drift tube and its accessories. This work paved the way towards further miniaturization of DT-IMS without compromise of performance.

SUBMITTER: Li L

PROVIDER: S-EPMC9269308 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer.

Project description:Elucidating the structures and stabilities of proteins and their complexes is paramount to understanding their biological functions in cellular processes. Native mass spectrometry (MS) coupled with ion mobility spectrometry (IMS) is emerging as an important biophysical technique owing to its high sensitivity, rapid analysis time, and ability to interrogate sample complexity or heterogeneity and the ability to probe protein structure dynamics. Here, a commercial IMS-MS platform has been modified for static native ESI emitters and an extended mass-to-charge range (20 kDa m/z) and its performance capabilities and limits were explored for a range of protein and protein complexes. The results show new potential for this instrument platform for studies of large protein and protein complexes and provides a roadmap for extending the performance metrics for studies of even larger, more complex systems, namely, membrane protein complexes and their interactions with ligands.

| S-EPMC7289629 | biostudies-literature

Conformational ordering of biomolecules in the gas phase: nitrogen collision cross sections measured on a prototype high resolution drift tube ion mobility-mass spectrometer.

Project description:Ion mobility-mass spectrometry measurements which describe the gas-phase scaling of molecular size and mass are of both fundamental and pragmatic utility. Fundamentally, such measurements expand our understanding of intrinsic intramolecular folding forces in the absence of solvent. Practically, reproducible transport properties, such as gas-phase collision cross-section (CCS), are analytically useful metrics for identification and characterization purposes. Here, we report 594 CCS values obtained in nitrogen drift gas on an electrostatic drift tube ion mobility-mass spectrometry (IM-MS) instrument. The instrument platform is a newly developed prototype incorporating a uniform-field drift tube bracketed by electrodynamic ion funnels and coupled to a high resolution quadrupole time-of-flight mass spectrometer. The CCS values reported here are of high experimental precision (±0.5% or better) and represent four chemically distinct classes of molecules (quaternary ammonium salts, lipids, peptides, and carbohydrates), which enables structural comparisons to be made between molecules of different chemical compositions for the rapid "omni-omic" characterization of complex biological samples. Comparisons made between helium and nitrogen-derived CCS measurements demonstrate that nitrogen CCS values are systematically larger than helium values; however, general separation trends between chemical classes are retained regardless of the drift gas. These results underscore that, for the highest CCS accuracy, care must be exercised when utilizing helium-derived CCS values to calibrate measurements obtained in nitrogen, as is the common practice in the field.

| S-EPMC3931330 | biostudies-literature

Performance evaluation of in-source ion activation hardware for collision-induced unfolding of proteins and protein complexes on a drift tube ion mobility-mass spectrometer.

Project description:Native ion mobility-mass spectrometry (IM-MS) has emerged as an information-rich technique for gas phase protein structure characterization; however, IM resolution is currently insufficient for the detection of subtle structural differences in large biomolecules. This challenge has spurred the development of collision-induced unfolding (CIU) which utilizes incremental gas phase activation to unfold a protein in order to expand the number of measurable descriptors available for native protein ions. Although CIU is now routinely used in native mass spectrometry studies, the interlaboratory reproducibility of CIU has not been established. Here we evaluate the reproducibility of the CIU data produced across three laboratories (University of Michigan, Texas A&M University, and Vanderbilt University). CIU data were collected for a variety of protein ions ranging from 8.6-66 kDa. Within the same laboratory, the CIU fingerprints were found to be repeatable with root mean square deviation (RMSD) values of less than 5%. Collision cross section (CCS) values of the CIU intermediates were consistent across the laboratories, with most features exhibiting an interlaboratory reproducibility of better than 1%. In contrast, the activation potentials required to induce protein CIU transitions varied between the three laboratories. To address these differences, three source assemblies were constructed with an updated ion activation hardware design utilizing higher mechanical tolerance specifications. The production-grade assemblies were found to produce highly consistent CIU data for intact antibodies, exhibiting high precision ion CCS and CIU transition values, thus opening the door to establishing databases of CIU fingerprints to support future biomolecular classification efforts.

| S-EPMC10103148 | biostudies-literature

Flexible Drift Tube for High Resolution Ion Mobility Spectrometry (Flex-DT-IMS).

Project description:This paper describes, in detail, the development of a novel, low-cost, and flexible drift tube (DT) along with an associated ion mobility spectrometer system. The DT is constructed from a flexible printed circuit board (PCB), with a bespoke "dog-leg" track design, that can be rolled up for ease of assembly. This approach incorporates a shielding layer, as part of the flexible PCB design, and represents the minimum dimensional footprint conceivable for a DT. The low thermal mass of the polyimide substrate and overlapping electrodes, as afforded by the dog-leg design, allow for efficient heat management and high field linearity within the tube-achieved from a single PCB. This is further enhanced by a novel double-glazing configuration which provides a simple and effective means for gas management, minimizing thermal variation within the assembly. Herein, we provide a full experimental characterization of the flexible DT ion mobility spectrometer (Flex-DT-IMS) with corresponding electrodynamic (Simion 8.1) and fluid dynamic (SolidWorks) simulations. The Flex-DT-IMS is shown to have a resolution >80 and a detection limit of low nanograms for the analysis of common explosives (RDX, PETN, HMX, and TNT).

| S-EPMC7467419 | biostudies-literature

Detection of nitro-based and peroxide-based explosives by fast polarity-switchable ion mobility spectrometer with ion focusing in vicinity of Faraday detector.

Project description:Ion mobility spectrometer (IMS) has been widely deployed for on-site detection of explosives. The common nitro-based explosives are usually detected by negative IMS while the emerging peroxide-based explosives are better detected by positive IMS. In this study, a fast polarity-switchable IMS was constructed to detect these two explosive species in a single measurement. As the large traditional Faraday detector would cause a trailing reactant ion peak (RIP), a Faraday detector with ion focusing in vicinity was developed by reducing the detector radius to 3.3?mm and increasing the voltage difference between aperture grid and its front guard ring to 591?V, which could remove trailing peaks from RIP without loss of signal intensity. This fast polarity-switchable IMS with ion focusing in vicinity of Faraday detector was employed to detect a mixture of 10?ng 2,4,6-trinitrotoluene (TNT) and 50?ng hexamethylene triperoxide diamine (HMTD) by polarity-switching, and the result suggested that [TNT-H](-) and [HMTD+H](+) could be detected in a single measurement. Furthermore, the removal of trailing peaks from RIP by the Faraday detector with ion focusing in vicinity also promised the accurate identification of KClO4, KNO3 and S in common inorganic explosives, whose product ion peaks were fairly adjacent to RIP.

| S-EPMC4448110 | biostudies-literature

An Interlaboratory Evaluation of Drift Tube Ion Mobility-Mass Spectrometry Collision Cross Section Measurements.

Project description:Collision cross section (CCS) measurements resulting from ion mobility-mass spectrometry (IM-MS) experiments provide a promising orthogonal dimension of structural information in MS-based analytical separations. As with any molecular identifier, interlaboratory standardization must precede broad range integration into analytical workflows. In this study, we present a reference drift tube ion mobility mass spectrometer (DTIM-MS) where improvements on the measurement accuracy of experimental parameters influencing IM separations provide standardized drift tube, nitrogen CCS values (DTCCSN2) for over 120 unique ion species with the lowest measurement uncertainty to date. The reproducibility of these DTCCSN2 values are evaluated across three additional laboratories on a commercially available DTIM-MS instrument. The traditional stepped field CCS method performs with a relative standard deviation (RSD) of 0.29% for all ion species across the three additional laboratories. The calibrated single field CCS method, which is compatible with a wide range of chromatographic inlet systems, performs with an average, absolute bias of 0.54% to the standardized stepped field DTCCSN2 values on the reference system. The low RSD and biases observed in this interlaboratory study illustrate the potential of DTIM-MS for providing a molecular identifier for a broad range of discovery based analyses.

| S-EPMC5744684 | biostudies-literature

Single-tube analysis for ultra-fast and visual detection of Salmonella.

Project description:Herein, we developed an ultra-fast and visual single-tube nucleic acid detection approach, which combined the advantages of self-settling characteristics of chitosan-functionalized diatomaceous earth (CDE) and accelerated PCR (AC-PCR). DNA was rapidly extracted by CDE within 3 min for the next nucleic acid amplification based on the nucleic acid attached on the chitosan in pH = 5.0. Under the action of gravity, the DNA-enriched CDE self-sediments to the bottom of the tube could be directly used for AC-PCR to achieve single-tube extraction and amplification. Our method detected Salmonella culture fluids with a detection limit of 1 CFU/mL, which was 100-fold more sensitive than conventional method that have not undergone nucleic acid enrichment. Furthermore, it also displayed high specificity and sensitivity for a variety of spiked samples. The entire process could be completed within 17 min in a single tube, and in particular, the result was visualized by the naked eyes. Overall, it is an all-in-one detection strategy without the requirement of redundant procedure, which greatly improved the detection efficiency, and saved the time and the cost. With these advantages, the approach will supply a promising tool in the field of point-of-care testing for Salmonella and other foodborne pathogens.

| S-EPMC8788404 | biostudies-literature

Ultra-fast photodetectors based on high-mobility indium gallium antimonide nanowires.

Project description:Because of tunable bandgap and high carrier mobility, ternary III-V nanowires (NWs) have demonstrated enormous potential for advanced applications. However, the synthesis of large-scale and highly-crystalline InxGa1-xSb NWs is still a challenge. Here, we achieve high-density and crystalline stoichiometric InxGa1-xSb (0.09 < x < 0.28) NWs on amorphous substrates with the uniform phase-purity and <110 >-orientation via chemical vapor deposition. The as-prepared NWs show excellent electrical and optoelectronic characteristics, including the high hole mobility (i.e. 463 cm2 V-1 s-1 for In0.09Ga0.91Sb NWs) as well as broadband and ultrafast photoresponse over the visible and infrared optical communication region (1550 nm). Specifically, the In0.28Ga0.72Sb NW device yields efficient rise and decay times down to 38 and 53 μs, respectively, along with the responsivity of 6000 A W-1 and external quantum efficiency of 4.8 × 106 % towards 1550 nm regime. High-performance NW parallel-arrayed devices can also be fabricated to illustrate their large-scale device integrability for next-generation, ultrafast, high-responsivity and broadband photodetectors.

| S-EPMC6458123 | biostudies-literature

Resolving structural isomers of monosaccharide methyl glycosides using drift tube and traveling wave ion mobility mass spectrometry.

Project description:Monosaccharide structural isomers including sixteen methyl-D-glycopyranosides and four methyl-N-acetylhexosamines were subjected to ion mobility measurements by electrospray ion mobility mass spectrometry. Two ion mobility-MS systems were employed: atmospheric pressure drift tube ion mobility time-of-flight mass spectrometry and a Synapt G2 HDMS system which incorporates a low pressure traveling wave ion mobility separator. All the compounds were investigated as [M + Na](+) ions in the positive mode. A majority of the monosaccharide structural isomers exhibited different mobility drift times in either system, depending on differences in their anomeric and stereochemical configurations. In general, drift time patterns (relative drift times of isomers) matched between the two instruments. Higher resolving power was observed using the atmospheric pressure drift tube. Collision cross section values of monosaccharide structural isomers were directly calculated from the atmospheric pressure ion mobility experiments, and a collision cross section calibration curve was made for the traveling wave ion mobility instrument. Overall, it was demonstrated that ion mobility-mass spectrometry using either drift tube or traveling wave ion mobility is a valuable technique for resolving subtle variations in stereochemistry among the sodium adducts of monosaccharide methyl glycosides.

| S-EPMC3633476 | biostudies-literature

Automated flow injection method for the high precision determination of drift tube ion mobility collision cross sections.

Project description:The field of ion mobility-based omics studies requires high-quality collision cross section (CCS) libraries to effectively utilize CCS as a molecular descriptor. Absolute CCS values with the highest precision are obtained on drift tube instruments by measuring the drift time of ions at multiple drift voltages, commonly referred to as a 'stepped field' experiment. However, generating large scale absolute CCS libraries from drift tube instruments is time consuming due to the current lack of high-throughput methods. This communication reports a fully automated stepped-field method to acquire absolute CCS on commercially available equipment. Using a drift tube ion mobility-mass spectrometer (DTIM-MS) coupled to a minimally modified liquid chromatography (LC) system, CCS values can be measured online with a carefully timed flow injection analysis (FIA) experiment. Results demonstrate that the FIA stepped-field method yields CCS values which are of high analytical precision (<0.4% relative standard deviation, RSD) and accuracy (?0.4% difference) comparable to CCS values obtained using traditional direct-infusion stepped-field experiments. This high-throughput CCS method consumes very little sample volume (20 ?L) and will expedite the generation of large-scale CCS libraries to support molecular identification within global untargeted studies.

| S-EPMC5869168 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data