12 results on '"Robin H. J. Kemperman"'
Search Results
2. Separation of Structurally Similar Anabolic Steroids as Cation Adducts in FAIMS-MS
- Author
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Michael S. Wei, Richard A. Yost, Michelle A. Palumbo, and Robin H. J. Kemperman
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Chromatography ,Anabolism ,Chemistry ,010401 analytical chemistry ,010402 general chemistry ,Anabolic-Androgenic Steroids ,01 natural sciences ,Mass Spectrometry ,0104 chemical sciences ,Adduct ,Structural Biology ,Cations ,Ion Mobility Spectrometry ,Testosterone Congeners ,human activities ,Spectroscopy - Abstract
Novel synthetic anabolic androgenic steroids have been developed not only to dodge current antidoping tests at the professional sports level, but also for consumption by noncompetitive bodybuilders. These novel anabolic steroids are commonly referred to as "designer steroids" and pose a significant risk to users because of the lack of testing for toxicity and safety in animals or humans. Manufacturers of designer steroids dodge regulation by distributing them as nutritional or dietary supplements. Improving the throughput and accuracy of screening tests would help regulators to stay on top of illicit anabolic steroids. High-field asymmetric-waveform ion mobility spectrometry (FAIMS) utilizes an alternating asymmetric electric field to separate ions by their different mobilities at high- and low-fields as they travel through the separation space. When coupled to mass spectrometry (MS), FAIMS enhances the separation of analytes from other interfering compounds with little to no increase in analysis time. Here we investigate the effects of adding various cation species to sample solutions for the separation of structurally similar or isomeric anabolic androgenic steroids. FAIMS-MS spectra for these cation-modified samples show an increased number of compensation field (CF) peaks, some of which are confirmed to be unique for one steroid isomer over another. The CF peaks observed upon addition of cation species correspond to both monomer steroid-cation adduct ions and larger multimer ion complexes. Notably, the number of CF peaks and their CF shifts do not appear to have a straightforward relationship with cation size or electronegativity. Future directions aim at investigating the structures for these analyte-cation adduct ions for building a predictive model for their FAIMS separations.
- Published
- 2020
3. A rapid and robust method for amino acid quantification using a simple N-hydroxysuccinimide ester derivatization and liquid chromatography-ion mobility-mass spectrometry
- Author
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Taylor M, Domenick, Austin L, Jones, Robin H J, Kemperman, and Richard A, Yost
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Metabolomics ,Succinimides ,Esters ,Amines ,Amino Acids ,Mass Spectrometry ,Chromatography, Liquid - Abstract
The vast majority of mass spectrometry (MS)-based metabolomics studies employ reversed-phase liquid chromatography (RPLC) to separate analytes prior to MS detection. Highly polar metabolites, such as amino acids (AAs), are poorly retained by RPLC, making quantitation of these key species challenging across the broad concentration ranges typically observed in biological specimens, such as cell extracts. To improve the detection and quantitation of AAs in microglial cell extracts, the implementation of a 4-dimethylaminobenzoylamido acetic acid N-hydroxysuccinimide ester (DBAA-NHS) derivatization agent was explored for its ability to improve both analyte retention and detection limits in RPLC-MS. In addition to the introduction of the DBAA-NHS labeling reagent, a uniformly (U)
- Published
- 2021
4. Deconvoluting the Proteome with Confidence Using Mass Spectrometric Tools
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Emily L Gill and Robin H J Kemperman
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Biochemistry (medical) ,Clinical Biochemistry - Published
- 2022
5. Rapid Quantitation of 25-Hydroxyvitamin D2 and D3 in Human Serum Using Liquid Chromatography/Drift Tube Ion Mobility-Mass Spectrometry
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Christopher D. Chouinard, Richard A. Yost, Jiajun Lei, Nicholas R Oranzi, Robin H. J. Kemperman, Timothy J. Garrett, and Brett Holmquist
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25-Hydroxyvitamin D 2 ,Drift tube ,Chromatography ,Ion-mobility spectrometry ,Extramural ,Chemistry ,010401 analytical chemistry ,Albumin ,Reproducibility of Results ,Reference Standards ,010402 general chemistry ,Mass spectrometry ,01 natural sciences ,0104 chemical sciences ,Analytical Chemistry ,Ion ,Liquid chromatography–mass spectrometry ,Limit of Detection ,Tandem Mass Spectrometry ,Ionization ,Ion Mobility Spectrometry ,Humans ,Epimer ,Calcifediol ,Chromatography, Liquid - Abstract
Ion mobility was integrated with liquid chromatography/high resolution mass spectrometry (LC/IM-HRMS) to quantify 25-hydroxyvitamin D (25OHD) in human serum. It has previously been shown that 25OHD adopts two gas-phase conformations which are resolved using ion mobility; in contrast, the inactive epimer, 3-epi-25-hydroxyvitamin D (epi25OHD) only adopts one. Interference from epi25OHD was eliminated by filtering the chromatogram to retain the drift time that corresponds to the unique gas-phase conformation of 25OHD. Although ion mobility separates the epimers, some chromatography is required to separate compounds which interfere with ionization or fall at the same nominal m/z. Standards were prepared in 4% albumin solutions and compared against commercial serum quality controls. Standards and quality controls were analyzed and validated using a two-minute LC/IM-MS method. 25-hydroxyvitamin D3 and D2 were quantified over the range between 2 and 500 ng/mL with bias and precision within 15%. When epi25OHD was spiked into quality control samples, no significant bias was introduced, and analysis of 30 patient samples shows good agreement between this LC/IM-MS and traditional LC/MS/MS methods. This work shows that ion mobility can be incorporated with liquid chromatography and mass spectrometry for rapid quantitation of 25OHD in human serum.
- Published
- 2019
6. Recent progress in metabolomics using ion mobility-mass spectrometry
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Nicholas R Oranzi, Richard A Yost, Allison J. Levy, Robin H. J. Kemperman, Michael S. Wei, and Atiye Ahmadireskety
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Chemical noise ,Chemistry ,Ion-mobility spectrometry ,010401 analytical chemistry ,Disease progression ,Structural diversity ,Computational biology ,01 natural sciences ,0104 chemical sciences ,Analytical Chemistry ,Metabolomics ,Lipidomics ,Direct analysis ,Spectroscopy ,Targeted metabolomics - Abstract
In recent years, metabolomics and lipidomics approaches have become increasingly popular for use in the analysis of human heath, molecular mechanisms, and disease progression. Despite the growth in applications and advances in instrumentation, metabolomics and lipidomics are limited by factors including interference from matrix effects, the need for lengthy for chromatographic analysis, and structural diversity of metabolites and lipids creating interference of isomers and isobars, which can confound identification. Ion mobility spectrometry (IMS) provides a method to enhance throughput, enhance isomeric separation, and reduce chemical noise. This review focuses on (i) the use of IMS and subsequent advancements in global metabolomics and lipidomics, (ii) the application and benefits of IMS in targeted metabolomics studies, and (iii) the use of IMS for non-chromatographic methods such as direct analysis, desorption ionization methods, and imaging.
- Published
- 2019
7. Effects of Solvent Vapor Modifiers for the Separation of Opioid Isomers in Micromachined FAIMS-MS
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Michael S. Wei, Richard A Yost, and Robin H. J. Kemperman
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Resolution (mass spectrometry) ,Ion-mobility spectrometry ,010401 analytical chemistry ,Inorganic chemistry ,010402 general chemistry ,Mass spectrometry ,01 natural sciences ,0104 chemical sciences ,Ion ,Solvent ,chemistry.chemical_compound ,chemistry ,Structural Biology ,Acetone ,Acetonitrile ,Spectroscopy ,Water vapor - Abstract
Opioid addiction is an escalating problem that is compounded by the introduction of synthetic opiate analogues such as fentanyl. Screening methods for these compound classes are challenged by the availability of synthetically manufactured analogues, including isomers of existing substances. High-field asymmetric-waveform ion mobility spectrometry (FAIMS) utilizes an alternating asymmetric electric field to separate ions by their different mobilities at high and low fields as they travel through the separation space. When coupled to mass spectrometry (MS), FAIMS enhances the separation of analytes from other interfering compounds with little to no increase in analysis time. Addition of solvent vapor into the FAIMS carrier gas has been demonstrated to enable and improve the separation of isomers. Here we investigate the effects of several solvents for the separation of four opioids. FAIMS-MS spectra with added solvent vapors show dramatic compensation field (CF) shifts for opioid [M+H]+ ions when compared to spectra acquired using dry nitrogen. Addition of vapor from aprotic solvents, such as acetonitrile and acetone, produces significantly improved resolution between the tested opioids, with baseline resolution achieved between certain opioid isomers. For protic solvents, notable CF shift differences were observed in FAIMS separations between addition of water vapor and vapors from small alcohols. Graphical Abstract.
- Published
- 2019
8. Ion mobility-mass spectrometry separation of steroid structural isomers and epimers
- Author
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Robin H. J. Kemperman, Christopher D. Chouinard, Harrison M. King, Christopher R. Beekman, and Richard A. Yost
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Resolution (mass spectrometry) ,Chemistry ,Ion-mobility spectrometry ,Dimer ,010401 analytical chemistry ,Analytical chemistry ,Protonation ,010402 general chemistry ,Mass spectrometry ,01 natural sciences ,Medicinal chemistry ,0104 chemical sciences ,Adduct ,chemistry.chemical_compound ,Structural isomer ,Chirality (chemistry) ,Spectroscopy - Abstract
Drift tube ion mobility spectrometry (DTIMS) coupled with mass spectrometry was evaluated for its capabilities in rapid separation of endogenous isomeric steroids. These compounds, which included eight isomer groups, were investigated as protonated and sodiated species and collision cross sections were measured for all ionization species of each steroid. Pregnenolone (CCSN2 176.7 A2) and 5α-dihydroprogesterone (CCSN2 191.4 A2) could be separated as protonated species, and aldosterone (CCSN2 197.7 A2) and cortisone (CCSN2 211.7 A2) could be separated as sodiated monomers. However, the sodiated dimers of the remaining isomers yielded increased separation, resulting in baseline resolution. Specific structural differences including ring conformation and the chirality of hydroxyl groups were compared to evaluate their relative effects on collision cross section in isomers. These results indicated that C5 ring conformation isomers androsterone and etiocholanolone, which both contain a C3 α-hydroxyl group, yielded similar dimer CCS. Yet these compounds were well resolved from their respective β-hydroxyl epimers, trans-androsterone and epietiocholanolone. Alternative drift gases were evaluated, and carbon dioxide drift gas offered slight improvement in isomer resolution well, including allowing separation of testosterone (CCSCO2 330.0 A2), dehydroepiandrosterone (CCSCO2 312.6 A2), and epitestosterone (CCSCO2 305.6 A2). Finally, different metal cation adducts, including alkali, alkaline earth, and first row transition metal adducts were analyzed, and several of these species provided improved resolution between steroid epimers. Overall, this study shows that drift tube ion mobility is a promising tool for improved separation of isomeric steroids.
- Published
- 2016
9. Measuring the Integrity of Gas-Phase Conformers of Sodiated 25-Hydroxyvitamin D3 by Drift Tube, Traveling Wave, Trapped, and High-Field Asymmetric Ion Mobility
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Nicholas R Oranzi, Michael S. Wei, Scott W Granato, Benjamin Rochon, Kevin Jeanne Dit Fouque, Francisco Fernandez-Lima, Julia L. Kaszycki, Aurelio La Rotta, Robin H. J. Kemperman, Richard A Yost, and Violeta I. Petkovska
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Drift tube ,Resolution (mass spectrometry) ,Chemistry ,Ion-mobility spectrometry ,010401 analytical chemistry ,Analytical chemistry ,Molecular Conformation ,010402 general chemistry ,Mass spectrometry ,01 natural sciences ,Mass Spectrometry ,0104 chemical sciences ,Analytical Chemistry ,Ion ,Ion Mobility Spectrometry ,Traveling wave ,Humans ,Epimer ,Biological Assay ,Vitamin D ,Conformational isomerism - Abstract
Quantitation of the serum concentration of 25-hydroxyvitamin D is a high-demand assay that suffers from long chromatography time to separate 25-hydroxyvitamin D from its inactive epimer; however, ion mobility spectrometry can distinguish the epimer pair in under 30 ms due to the presence of a unique extended or "open" gas-phase sodiated conformer, not shared with the epimer, reducing the need for chromatographic separation. Five ion mobility mass spectrometers utilizing commercially available IMS technologies, including drift tube, traveling wave, trapped, and high-field asymmetric ion mobility spectrometry, are evaluated for their ability to resolve the unique open conformer. Additionally, settings for each instrument are evaluated to understand their influence on ion heating, which can drive the open conformer into a compact or "closed" conformer shared with the epimer. The four low-field instruments successfully resolved the open conformer from the closed conformer at baseline or near-baseline resolution at typical operating parameters. High-field asymmetric ion mobility was unable to resolve a unique peak but detected two peaks for the epimer, in contrast to the low-field methods that detected one conformer. This study seeks to expand the instrument space by highlighting the potential of each platform for the separation of 25-hydroxyvitamin D epimers.
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- 2019
10. Ion Mobility in Clinical Analysis: Current Progress and Future Perspectives
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Richard A. Yost, Michael S. Wei, Christopher D. Chouinard, Christopher R. Beekman, and Robin H. J. Kemperman
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Ions ,Clinical Laboratory Techniques ,Ion-mobility spectrometry ,business.industry ,Chemistry ,010401 analytical chemistry ,Biochemistry (medical) ,Clinical Biochemistry ,Future application ,Nanotechnology ,010402 general chemistry ,Mass spectrometry ,01 natural sciences ,Mass spectrometric ,Mass Spectrometry ,0104 chemical sciences ,Ion ,Characterization (materials science) ,Humans ,Metabolomics ,Instrumentation (computer programming) ,Current (fluid) ,Process engineering ,business - Abstract
BACKGROUND Ion mobility spectrometry (IMS) is a rapid separation tool that can be coupled with several sampling/ionization methods, other separation techniques (e.g., chromatography), and various detectors (e.g., mass spectrometry). This technique has become increasingly used in the last 2 decades for applications ranging from illicit drug and chemical warfare agent detection to structural characterization of biological macromolecules such as proteins. Because of its rapid speed of analysis, IMS has recently been investigated for its potential use in clinical laboratories. CONTENT This review article first provides a brief introduction to ion mobility operating principles and instrumentation. Several current applications will then be detailed, including investigation of rapid ambient sampling from exhaled breath and other volatile compounds and mass spectrometric imaging for localization of target compounds. Additionally, current ion mobility research in relevant fields (i.e., metabolomics) will be discussed as it pertains to potential future application in clinical settings. SUMMARY This review article provides the authors' perspective on the future of ion mobility implementation in the clinical setting, with a focus on ambient sampling methods that allow IMS to be used as a “bedside” standalone technique for rapid disease screening and methods for improving the analysis of complex biological samples such as blood plasma and urine.
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- 2016
11. Cation-Dependent Conformations in 25-Hydroxyvitamin D3-Cation Adducts Measured by Ion Mobility-Mass Spectrometry and Theoretical Modeling
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Robin H. J. Kemperman, Adrian E. Roitberg, Nicholas R Oranzi, Richard A. Yost, Vinícius Wilian D. Cruzeiro, and Christopher D. Chouinard
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010401 analytical chemistry ,010402 general chemistry ,Condensed Matter Physics ,Mass spectrometry ,01 natural sciences ,Article ,0104 chemical sciences ,Adduct ,Ion ,Gibbs free energy ,chemistry.chemical_compound ,symbols.namesake ,Monomer ,chemistry ,Computational chemistry ,symbols ,Molecule ,Epimer ,Physical and Theoretical Chemistry ,Instrumentation ,Conformational isomerism ,Spectroscopy - Abstract
Ion mobility-mass spectrometry is a useful tool in separation of biological isomers, including clinically relevant analytes such as 25-hydroxyvitamin D3 (25OHD3) and its epimer, 3-epi-25-hydroxyvitamin D3 (epi25OHD3). Previous research indicates that these epimers adopt different gas-phase sodiated monomer structures, either the “open” or “closed” conformer, which allow 25OHD3 to be readily resolved in mixtures. In the current work, alternative metal cation adducts are investigated for their relative effects on the ratio of “open” and “closed” conformers. Alkali and alkaline earth metal adducts caused changes in the 25OHD3 conformer ratio, where the proportion of the “open” conformer generally increases with the size of the metal cation in a given group. As such, the ratio of the “open” conformer, which is unique to 25OHD3 and absent for its epimer, can be increased from approximately 1:1 for the sodiated monomer to greater than 8:1 for the barium adduct. Molecular modeling and energy calculations agree with the experimental results, indicating that the Gibbs free energy of conversion from the “closed” to the “open” conformation decreased with increasing cation size, correlating with the variation in ratio between the conformers. This work demonstrates the effect of cation adducts on gas-phase conformations of small, flexible molecules and offers an additional strategy for resolution of clinically relevant epimers.
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- 2018
12. Portable FAIMS: Applications and Future Perspectives
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Richard A. Yost, Michael T. Costanzo, Christopher R. Beekman, Michael S. Wei, Jared J. Boock, and Robin H. J. Kemperman
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Chemistry ,business.industry ,Ion-mobility spectrometry ,010401 analytical chemistry ,Analytical chemistry ,010402 general chemistry ,Condensed Matter Physics ,01 natural sciences ,Method development ,Article ,0104 chemical sciences ,Software portability ,In situ analysis ,Instrumentation (computer programming) ,Physical and Theoretical Chemistry ,business ,Instrumentation ,Throughput (business) ,Spectroscopy ,Computer hardware - Abstract
Miniaturized mass spectrometry (MMS) is optimal for a wide variety of applications that benefit from field-portable instrumentation. Like MMS, field asymmetric ion mobility spectrometry (FAIMS) has proven capable of providing in situ analysis, allowing researchers to bring the lab to the sample. FAIMS compliments MMS very well, but has the added benefit of operating at atmospheric pressure, unlike MS. This distinct advantage makes FAIMS uniquely suited for portability. Since its inception, FAIMS has been envisioned as a field-portable device, as it affords less expense and greater simplicity than many similar methods Ideally, these are simple, robust devices that may be operated by non-professional personnel, yet still provide adequate data when in the field. While reducing the size and complexity tends to bring with it a loss of performance and accuracy, this is made up for by the incredibly high throughput and overall convenience of the instrument. Moreover, the FAIMS device used in the field can be brought back to the lab, and coupled to a conventional mass spectrometer to provide any necessary method development and compound validation. This work discusses the various considerations, uses, and applications for portable FAIMS instrumentation, and how the future of each applicable field may benefit from the development and acceptance of such a device.
- Published
- 2018
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