Isomeric Oligosaccharides Analyses Using Negative-ion Electrospray Ionization Ion Mobility Spectrometry Combined with Collision-induced Dissociation MS/MS

Yamagaki, Tohru; Sato, Akihiro

doi:10.2116/analsci.25.985

Cited by 42 publications

(30 citation statements)

References 17 publications

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“…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. Isomer separation of small carbohydrates has been demonstrated [22][23][24][25][26][27] but, with current technology, the resolution of the mobility cells is not sufficient to resolve any but the smaller N-glycans [15,28]. For a review on instrumentation see [29].…”

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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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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“…Successful approaches trying to improve the situation, with special focus on the resolving power of IMS devices, concentrated especially on the electron source and the voltage schemes applied to the device. Regarding the electron source, prominent examples are electrospray ionization (typically for liquid samples) (Wittmer et al 1994, Chen et al 1996, Wu et al 2000, Harris et al 2008, Yamagaki and Sato 2009, optical sources (high-intensity light sources resp. laser, X-ray) (Matsaev et al 2002, Sielemann et al 2002, Oberh ü ttinger et al 2009 ), corona discharges (Tabrizchi et al 2000, Schmidt et al 2001, Khayamian et al 2003, Han et al 2007, Mulugeta et al 2010, Tabrizchi and Ilbeigi 2010, and electron guns (Gunzer et al 2010a ).…”

Section: Introductionmentioning

confidence: 99%

Pulsed electron beams in ion mobility spectrometry

Baether¹,

Zimmermann²,

Gunzer³

2012

Reviews in Analytical Chemistry

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Abstract:Ion mobility spectrometry is a well-known technique used to analyze trace gases in ambient air. Typically, it works by employing a radioactive source to provide electrons with high energy to ionize the analytes in a series of chemical reactions. During the past ten years non-radioactive sources have been one of the subjects of interest in ion mobility spectrometry, initially in order to replace radioactive sources as a result of general security and regulatory concerns. Among these non-radioactive sources especially pulsed sources have recently been shown to additionally improve the analytic information provided by ion mobility spectrometers. In this review we will describe the progress regarding the application of pulsed non-radioactive electron sources in ion mobility spectrometry and show the recent analytical advances that have been achieved by using pulsed electron beams.

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“…The combination of collision induced dissociation (CID) with electron transfer dissociation (ETD) is making it possible to determine peptide sequences as well as glycan positions and structures [3]. Recently, ion mobility spectrometry (IMS) [6] has emerged as a means of separating isomers prior to MS analysis [7][8][9][10][11][12][13][14][15][16]. Because IMS separates ions based on their shapes, it also offers information that is complementary to MS analysis.…”

Section: Introductionmentioning

confidence: 99%

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Bohrer

Clemmer

2011

J. Am. Soc. Mass Spectrom.

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The binding properties of a peptidoglycan recognition protein are translated via combinatorial chemistry into short peptides. Non-adjacent histidine, tyrosine, and arginine residues in the protein's binding cleft that associate specifically with the glycan moiety of a peptidoglycan substrate are incorporated into linear sequences creating a library of 27 candidate tripeptide reagents (three possible residues permutated across three positions). Upon electrospraying the peptide library and carbohydrate mixtures, some noncovalent complexes are observed. The binding efficiencies of the peptides vary according to their amino acid composition as well as the disaccharide linkage and carbohydrate ring-type. In addition to providing a charge-carrier for the carbohydrate, peptide reagents can also be used to differentiate carbohydrate isomers by ion mobility spectrometry. The utility of these peptide reagents as a means of enhancing ion mobility analysis of carbohydrates is illustrated by examining four glucose-containing disaccharide isomers, including a pair that is not resolved by ion mobility alone. The specificity and stoichiometry of the peptide-carbohydrate complexes are also investigated. Trihistidine demonstrates both suitable binding efficiency and successful resolution of disaccharides isomers, suggesting it may be a useful reagent in IMS analyses of carbohydrates.

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Isomeric Oligosaccharides Analyses Using Negative-ion Electrospray Ionization Ion Mobility Spectrometry Combined with Collision-induced Dissociation MS/MS

Cited by 42 publications

References 17 publications

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

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

Pulsed electron beams in ion mobility spectrometry

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

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