Biomolecular structural separations by ion mobility–mass spectrometry

Fenn, Larissa S.; McLean, John A.

doi:10.1007/s00216-008-1951-x

Cited by 142 publications

(151 citation statements)

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“…Biomolecular ion structure analysis utilizing IMS has an extensive history [19,20,[30][31][32]. The development of IMS instrumentation [20,[33][34][35][36][37][38][39][40], theory [41][42][43][44][45], and applications [46][47][48][49][50] is described in the literature.…”

Section: Ims-ms Measurementsmentioning

confidence: 99%

Gas-Phase Hydrogen-Deuterium Exchange Labeling of Select Peptide Ion Conformer Types: a Per-Residue Kinetics Analysis

Khakinejad

Kondalaji

Tafreshian

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. The per-residue, gas-phase hydrogen deuterium exchange (HDX) kinetics for individual amino acid residues on selected ion conformer types of the model peptide KKDDDDDIIKIIK have been examined using ion mobility spectrometry (IMS) and HDX-tandem mass spectrometry (MS/MS) techniques. The [M + 4H] 4+ ions exhibit two major conformer types with collision cross sections of 418 Å 2 and 446 Å 2 ; the [M + 3H] 3+ ions also yield two different conformer types having collision cross sections of 340 Å 2 and 367 Å 2 . Kinetics plots of HDX for individual amino acid residues reveal fast-and slow-exchanging hydrogens. The contributions of each amino acid residue to the overall conformer type rate constant have been estimated. For this peptide, N-and C-terminal K residues exhibit the greatest contributions for all ion conformer types. Interior D and I residues show decreased contributions. Several charge state trends are observed. On average, the D residues of the [M + 3H] 3+ ions show faster HDX rate contributions compared with [M + 4H] 4+ ions. In contrast the interior I8 and I9 residues show increased accessibility to exchange for the more elongated [M + 4H] 4+ ion conformer type. The contribution of each residue to the overall uptake rate showed a good correlation with a residue hydrogen accessibility score model calculated using a distance from charge site and initial incorporation site for nominal structures obtained from molecular dynamic simulations (MDS).

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Section: Ims-ms Measurementsmentioning

confidence: 99%

Gas-Phase Hydrogen-Deuterium Exchange Labeling of Select Peptide Ion Conformer Types: a Per-Residue Kinetics Analysis

Khakinejad

Kondalaji

Tafreshian

et al. 2015

J. Am. Soc. Mass Spectrom.

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“…For example, Fenn and McLean [16][17][18] have shown that compounds of different structural types such as lipids, peptides and carbohydrates can be separated and, recently, this group has applied the technique to examination of N-linked glycans released from ribonuclease B [18]. Ion mobility separation coupled with principal component analysis of N-linked glycans from serum glycoproteins has shown promise for detection of cancer biomarkers [19] and ion mobility separations have also been used to examine N-linked glycan heterogeniety from monoclonal antibodies [20,21] although, in these cases, glycopeptides rather than the released glycans were examined.…”

Section: Introductionmentioning

confidence: 99%

Ion Mobility Mass Spectrometry for Extracting Spectra of N-Glycans Directly from Incubation Mixtures Following Glycan Release: Application to Glycans from Engineered Glycoforms of Intact, Folded HIV gp120

Harvey

Sobott

Crispin

et al. 2011

J. Am. Soc. Mass Spectrom.

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The analysis of glycosylation from native biological sources is often frustrated by the low abundances of available material. Here, ion mobility combined with electrospray ionization mass spectrometry have been used to extract the spectra of N-glycans released with PNGase F from a serial titration of recombinantly expressed envelope glycoprotein, gp120, from the human immunodeficiency virus (HIV). Analysis was also performed on gp120 expressed in the α-mannosidase inhibitor, and in a matched mammalian cell line deficient in GlcNAc transferase I. Without ion mobility separation, ESI spectra frequently contained no observable ions from the glycans whereas ions from other compounds such as detergents and residual buffer salts were abundant. After ion mobility separation on a Waters T-wave ion mobility mass spectrometer, the N-glycans fell into a unique region of the ion mobility/m/z plot allowing their profiles to be extracted with good signal:noise ratios. This method allowed N-glycan profiles to be extracted from crude incubation mixtures with no clean-up even in the presence of surfactants such as NP40. Furthermore, this technique allowed clear profiles to be obtained from sub-microgram amounts of glycoprotein. Glycan profiles were similar to those generated by MALDI-TOF MS although they were more susceptible to double charging and fragmentation. Structural analysis could be accomplished by MS/MS experiments in either positive or negative ion mode but negative ion mode gave the most informative spectra and provided a reliable approach to the analysis of glycans from small amounts of glycoprotein.

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“…Journal of Lipid Research Volume 58, 2017 Ion mobility spectrometry (IMS) provides such orthogonal separation (19)(20)(21)(22)(23)(24). IMS separates ions on the basis of the mobility of the ions as they travel through a neutral background gas (most commonly helium and nitrogen), which is governed by the collision frequency between the ions and the neutral gas, i.e., the ion-neutral collision crosssection (CCS; ).…”

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confidence: 99%

Assessment of altered lipid homeostasis by HILIC-ion mobility-mass spectrometry-based lipidomics

Hines

Herron

2017

Journal of Lipid Research

117

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implicated in a number of human diseases, such as atherosclerosis (3), nonalcoholic fatty liver (4), diabetes (5), Alzheimer's disease (6), and cancer (7,8). Advances in lipidomic techniques and strategies, led by the LIPID MAPS consortium, have greatly enhanced our understanding of the distribution and biological roles of lipids (9-13). Modern mass spectrometry (MS), coupled with electrospray ionization (ESI), is the key to qualitative and quantitative lipidomic analysis. Typical MS-based lipidomic strategies are shotgun (i.e., direct infusion) lipidomics (9, 14) and liquid chromatography (LC)-MS lipidomics (11,15,16). Shotgun lipidomics relies on partial intrasource separation of lipid classes through varying the pH of the lipid solution and identification of lipid species by their characteristic fragmentation in tandem MS analysis (9,17). This approach has the advantage of being high-throughput, but it also has several disadvantages: a) suppression of low-abundant species by major polar lipids such as phosphatidylcholines; b) difficulty in analysis of lipid species that are poorly ionized by ESI; and c) inability to provide structural information on isobaric and isomeric species. The LC-MS-based strategy utilizes targeted analysis of each lipid class under conditions that are optimized for that particular class (11,15,16,18). This strategy has the advantages of being specific, sensitive, and comprehensive, but it also has limitations, such as being time consuming and less cost effective. To increase the throughput of the LC-MS lipidomics while maintaining the specificity and sensitivity, we desire improved chromatographic techniques and additional dimensions of separation that are orthogonal to LC and MS. Lipids play important roles in maintaining membrane structures and mediating signaling pathways (1, 2). Dysregulated lipid biosynthesis and metabolism have been Abstract Ion mobility-mass spectrometry (IM-MS) has proven to be a highly informative technique for the characterization of lipids from cells and tissues. We report the combination of hydrophilic-interaction liquid chromatography (HILIC) with traveling-wave IM-MS (TWIM-MS

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Biomolecular structural separations by ion mobility–mass spectrometry

Cited by 142 publications

References 20 publications

Gas-Phase Hydrogen-Deuterium Exchange Labeling of Select Peptide Ion Conformer Types: a Per-Residue Kinetics Analysis

Gas-Phase Hydrogen-Deuterium Exchange Labeling of Select Peptide Ion Conformer Types: a Per-Residue Kinetics Analysis

Ion Mobility Mass Spectrometry for Extracting Spectra of N-Glycans Directly from Incubation Mixtures Following Glycan Release: Application to Glycans from Engineered Glycoforms of Intact, Folded HIV gp120

Assessment of altered lipid homeostasis by HILIC-ion mobility-mass spectrometry-based lipidomics

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