• Mass Spectrometry Letters
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• 제8권4호
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• pp.79-89
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• 2017

Ion mobility mass spectrometry (IM-MS) combines the advantages of ion mobility spectrometry (IMS) and MS for effective gas-phase ion analysis. Separation of ions based on their mobilities prior to MS can be performed without a great loss in other analytical figures of merit, and the extra dimension of analysis offered by IM can be beneficial for isomer and complex sample analyses. In this review, basic principles of IMS and IM-MS are described in addition to an introduction to various IMS techniques and commercial IM-MS instruments. The nature of collision cross-section (${\Omega}_D$), an important parameter determining the transport properties of ions in IMS, is also explained in detail.

• Mass Spectrometry Letters
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• 제11권4호
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• pp.65-70
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• 2020

Despite its great success in the field of proteomics, mass spectrometry has limited use for determining structural details of peptides, proteins, and their assemblies. Emerging ion mobility spectrometry-mass spectrometry has enabled us to explore the conformational space of protein ions in the gas phase, and further combinations with the gas-phase ion spectroscopy and the collision-induced unfolding have extended its abilities to elucidating the secondary structure and local details of conformational transitions. This review will provide a brief introduction to the combined approaches of IMS-MS with gas-phase ion infrared spectroscopy or collision-induced unfolding and their most recent results that successfully revealed higher-order structural details.

• Mass Spectrometry Letters
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• 제12권4호
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• pp.137-145
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• 2021

Herein we report multiple ion mobility (IM) peaks in electrospray ionization IM mass spectrometry (ESI-IM-MS) produced by glutamine residue in peptide. The mobility features of 147 peptides were investigated using ESI-IM-MS combined with liquid chromatography. Of these peptides, 66 presented multiple IM peaks, and analysis of their sequence using collision induced dissociation (CID) revealed that glutamine (Gln), as well as proline (Pro), plays a critical role in generating multiple IM peaks. Mutant-based investigations using Gln-containing peptides indicate that the side chain of Gln promotes intermolecular interactions, inducing multiple structures of the peptide ions in the gas phase. Consequently, the present study demonstrates that the distinct ion mobility signatures identified herein can potentially be used to characterize glutamine-containing peptide ions.

• Mass Spectrometry Letters
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• 제12권4호
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• pp.152-158
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• 2021

Electrospray ionization (ESI) and ion mobility spectrometry-mass spectrometry (IMS-MS) were employed to investigate the solvated structures of ionic species in the lithium iodide electrolyte solution in the gas phase. The Li⁺I^-Li⁺ triple ion and single standalone Li+ ions solvated by 1,4-dioxane were successfully generated and observed by ESI-MS under the influence of dioxane vapor at the inlet region. Under the present experimental condition, (1,4-dioxane)_m·Li⁺ complex ions (m = 1, 2, and 3) and a (1,4-dioxane)·Li⁺I^-Li⁺ complex ion were observed, which were further examined by IMS to investigate their structures. The presence of multiple structural isomers was confirmed, which accounts for the endothermic conformational transition of 1,4-dioxane from a chair to a boat to achieve bidentate O-donor binding to Li⁺ and Li⁺I^-Li⁺. Further structural details critical for the ion-solvent interactions were also examined and discussed with the help of density functional theory calculations.

• Mass Spectrometry Letters
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• 제7권1호
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• pp.16-20
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• 2016

Characterization of intact protein structures in the gas phase using electrospray ionization combined with ion mobility mass spectrometry has become an important tool of research. However, the biophysical properties that govern the structures of protein ions in the gas phase remain to be understood. Here, we investigated the impact of host-guest complexation of ubiquitin (Ubq) with macrocyclic host molecules, cucurbit[n]urils (CB[n]s, n = 6, 7), on its structure in the gas phase. We found that CB[n] complexation induces the formation of compact Ubq ions. Both CB[6] and CB[7] exhibited similar effects despite differences in their binding properties in solution. In addition, CB[n] attachment prevented Ubq from unfolding by collisional activation. Based on the experimental results, we suggest that CB[n]s prevent unfolding of Ubq during transfer to the gas phase to promote the formation of compact protein ions. Furthermore, interaction with positively charged residues per se is suggested to be the most important factor for the host-guest complexation effect.

• Mass Spectrometry Letters
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• 제6권1호
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• pp.17-20
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• 2015

Sesamin, one of the lignans in sesame seed, was a labile compound in MS and it was reported that the protonated molecule of sesamin decomposed easily in ES ionization process and it cannot be detected (G. Yan, et al., Rapid Commun Mass Spectrom. 2007, 21, 3613-3620). To protect labile compounds, an amino-cyclodextrin (NCyD) was added to the sample to promote the host-guest interaction complex in ESI-MS. As a result, sesamin was ionized as the NCyD-sesamin-NCyD (1:2) complex without undesired decomposition, suggesting that the amino-CyDs assist the ionization of the labile molecules capped with CyDs by host-guest interaction and these compounds were ionized without their decomposition, those are like amino-CyD complex-assisted ionization. The amino-CyD complexes of sesamin and sesamolin were also analyzed by their ion-mobility MS.

• Bulletin of the Korean Chemical Society
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• 제32권3호
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• pp.1055-1058
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• 2011

• Bulletin of the Korean Chemical Society
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• 제35권4호
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• pp.1023-1028
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• 2014

Protonated caffeine ($CH^+$) and glucosamine ($GH^+$) overlapped in an analysis with ion mobility spectrometryquadrupole mass spectrometry. Ethyl lactate vapor (L) at different concentrations from 0 to 22 mmol $m^{-3}$ was added as a buffer gas modifier to separate these signals. The drift times of $CH^+$ and $GH^+$ increased with L concentration. The drift time increase was associated to clustering equilibria of $CH^+$ and $GH^+$ with one molecule of L and the equilibrium of $GH^+$ was more displaced to the formation of $GLH^+$ than that of $GLH^+$. $GH^+$ clustered more to L than $CH^+$ because $GLH^+$ formed more stable hydrogen bonds (26.30 kcal/mol) than $GLH^+$ (24.66 kcal/mol) and the positive charge in $GH^+$ was more sterically accessible than in $CH^+$. The aim of this work was to use theoretical calculations to guide the selection of a buffer gas modifier for IMS separations of two compounds that overlap in the mobility spectra and predict this separation, simplifying that empirical process.

• Bulletin of the Korean Chemical Society
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• 제31권8호
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• pp.2383-2385
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• 2010

• Mass Spectrometry Letters
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• 제15권1호
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• pp.1-25
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• 2024

Protein glycosylation, a highly significant and ubiquitous post-translational modification (PTM) in eukaryotic cells, has attracted considerable research interest due to its pivotal role in a wide array of essential biological processes. Conducting a comprehensive analysis of glycoproteins is imperative for understanding glycoprotein bio-functions and identifying glycosylated biomarkers. However, the complexity and heterogeneity of glycan structures, coupled with the low abundance and poor ionization efficiencies of glycopeptides have all contributed to making the analysis and subsequent identification of glycans and glycopeptides much more challenging than any other biopolymers. Nevertheless, the significant advancements in enrichment techniques, chromatographic separation, and mass spectrometric methodologies represent promising avenues for mitigating these challenges. Numerous substrates and multifunctional materials are being designed for glycopeptide enrichment, proving valuable in glycomics and glycoproteomics. Mass spectrometry (MS) is pivotal for probing protein glycosylation, offering sensitivity and structural insight into glycopeptides and glycans. Additionally, enhanced MS-based glycopeptide characterization employs various separation techniques like liquid chromatography, capillary electrophoresis, and ion mobility. In this review, we highlight recent advances in enrichment methods and MS-based separation techniques for analyzing different types of protein glycosylation. This review also discusses various approaches employed for glycan release that facilitate the investigation of the glycosylation sites of the identified glycoproteins. Furthermore, numerous bioinformatics tools aiding in accurately characterizing glycan and glycopeptides are covered.