Fragmentation of Sialylated Carbohydrates Using Infrared Atmospheric Pressure MALDI Ion Trap Mass Spectrometry from Cation-Doped Liquid Matrixes

Seggern, Christopher E. Von; Zarek, Paul E.; Cotter, Robert J.

doi:10.1021/ac0348367

Cited by 30 publications

(40 citation statements)

References 40 publications

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“…Ion fragments of the 0,2 A-type observed in the NAH GlcNAc residues containing 1¡4 linkage suggest the fragmentation mechanism is a retro-aldol rearrangement of oligosaccharide ions in the negative mode [32][33][34][35]. This mechanism requires an open-ring reducing terminal aldehyde, and such structures are formed by C-type fragmentation [34 -38].…”

Section: Resultsmentioning

confidence: 99%

Tandem MS can distinguish hyaluronic acid from N-acetylheparosan

Zhang

Xie

Liu³

et al. 2008

J. Am. Soc. Mass Spectrom.

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Isobaric oligosaccharides enzymatically prepared from hyaluronic acid (HA) and N-acetylheparosan (NAH), were distinguished using tandem mass spectrometry. The only difference between the two series of oligosaccharides was the linkage pattern (in HA 1¡3 and in NAH 1¡4) between glucuronic acid and N-acetylglucosamine residues. Tandem mass spectrometry afforded spectra in which glycosidic cleavage fragment ions were observed for both HA and NAH oligosaccharides. Cross-ring cleavage ions 0,2 A n and 0,2 A n -h (n is even number) were observed only in GlcNAc residues of NAH oligosaccharides. One exception was an 0,2 A 2 ion fragment observed for the disaccharide from HA. These cross-ring cleavage fragment ions are useful to definitively distinguish HA and NAH oligosaccharides. -3]. GAGs are divided into four main categories: hyaluronic acid or hyaluronan (HA), chondroitin/dermatan sulfate, Nacetylheparosan (NAH)/heparan sulfate/heparin, and keratan sulfate, based on their monosaccharide composition and the configuration and position of the glycosidic bonds between these monosaccharides. The specificity of the interactions between GAGs and proteins results from structural diversity of GAGs defined by their size, saccharide composition and sequence, charge density [4,5]. Thus, understanding the structure of a GAG is essential in understanding its activity and biological functions. HA and NAH are biosynthesized by both prokaryotic and eukaryotic cells. HA is copolymer linked polymer of ␤-1,4 D-glucuronic acid (GlcA) and ␤-1,3 D-N-acetylglucosamine (GlcNAc) [6]. NAH is a copolymer of ␤-1,4 GlcA and ␣-1,4 GlcNAc and the biosynthetic precursor of the mammalian GAGs, heparin and heparan sulfate [7]. HA can be prepared by bacterial fermentation of Streptococcus zooepidemicus [8], or enzymatically using biosynthetic enzymes prepared from Pasturella multocida [9]. Bacteria use HA as camouflage to enhance their ability to infect higher animals [10]. Similarly, Escherichia coli strain K5 produces capsular polysaccharide comprised of NAH [11]. NAH is also important as it represents a considerable portion of the sequence of mammalian heparan sulfate [12,13]. HA and NAH are the two simplest GAGs since neither has sulfo groups and, thus, consist of only a single sequence (Figure 1). HA and NAH have very similar structures, differing only in the position of their glycosidic linkage between GlcA and GlcNAc. This difference in structure results from very different biosynthesis pathways for HA and NAH [14 -17] and gives each polysaccharide unique biological functions and distinctive structure-activity relationships [18].The oligosaccharides prepared from GAGs by controlled enzymatic depolymerization are often studied to define the minimum structural requirements for biological activity [19,20]. ESI-MS is particularly useful to monitor these GAG-derived oligosaccharides due to its soft ionization [21,22]. LC-ESI-MS, relying on reversedphase ion-pairing (RPIP)-high-performance liquid chromatography (HPLC), has employed volatile ion-pai...

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Section: Resultsmentioning

confidence: 99%

Tandem MS can distinguish hyaluronic acid from N-acetylheparosan

Zhang

Xie

Liu³

et al. 2008

J. Am. Soc. Mass Spectrom.

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“…The results obtained during the present study indicate that applying a CMBT matrix solution on top of a co-crystallization of an analyte/2,5-DHB mixture facilitates high-resolution FTICR mass analysis of the high mass HMOS, without the occurrence of an unacceptable degree of fragmentation. Although increase in the local pressure during desorption [60–62] or analysis at atmospheric pressure [63] has proven to relieve the vibrational excitation introduced during the ionization/desorption of native oligosaccharides or glycoconjugates, such approaches did not appear to be necessary for this study, since selection of an optimum matrix preparation provided stabilization sufficient for profiling the permethylated oligosaccharides investigated here. Nevertheless, desorption/ionization at increased pressure could be useful when examination of even higher-molecular weight fractions is undertaken.…”

Section: Resultsmentioning

confidence: 99%

Mass spectrometric detection of multiple extended series of neutral highly fucosylated N-acetyllactosamine oligosaccharides in human milk

Pfenninger

Chan

Karas

et al. 2008

International Journal of Mass Spectrometry

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Complex mixtures of high molecular weight fractions of pooled neutral human milk oligosaccharides (obtained via gel permeation chromatography) have been investigated. The subfractions were each permethylated and analyzed by high-resolution mass spectrometry, using matrix-assisted laser desorption/ionization (MALDI)-Fourier transform ion cyclotron resonance (FTICR) mass spectrometry, in order to investigate their oligosaccharide compositions. The obtained spectra reveal that human milk contains more complex neutral oligosaccharides than have been described previously; the data show that these oligosaccharides can be highly fucosylated, and that their poly-N-acetyllactosamine cores are substituted with up to 10 fucose residues on a an oligosaccharide that has 7-N-acetyllactosamine units. This is the first report of the existence in human milk of this large range of highly fucosylated oligosaccharides which possess novel, potentially immunologically active structures.

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“…UV AP-MALDI coupled to an ion trap mass spectrometer was used by Creaser et al [275] to acquire MS n spectra of sodium adducts of neutral oligosaccharides and by Moyer et al for the negative mode analyses of sialylated oligosaccharides [276]. More recently, the analysis of sialylated oligosaccharides using infrared atmospheric pressure matrix assisted laser desorption/ionisation on an ion trap mass spectrometer (IR AP-MALDI-ITMS) has been reported [277,278]. This configuration makes use of the fact that the IR laser wavelength coincides with the O-H stretching frequency, and thus aqueous matrixes, such as water and glycerol; can be used.…”

Section: Fragmentation Of Glycansmentioning

confidence: 99%

Glycomics and Mass Spectrometry

Morelle¹,

Michalski

2005

CPD

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Proteomics is closely associated with the modifications of the gene product such as the post-translational events that yield functionally active gene products. Among these, glycosylation represents a critically important post-translational modification and is a target for proteomic research. Glycan moieties are involved in a wide variety of intracellular, cell-cell and cell-matrix recognition events. This is why understanding how glycosylation affects the activities and functions of proteins in health and disease represents a major challenge. The study of the glycome--the whole set of glycans produced in a single organism--is therefore essential to determine the functions of all genes. Mass spectrometry, in combination with modern separation methodologies, is one of the most powerful and versatile techniques for the structural analysis of oligosaccharides. This review provides a summary of the current knowledge for the mass spectrometric analysis of glycoproteins and their glycan structures.

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Fragmentation of Sialylated Carbohydrates Using Infrared Atmospheric Pressure MALDI Ion Trap Mass Spectrometry from Cation-Doped Liquid Matrixes

Cited by 30 publications

References 40 publications

Tandem MS can distinguish hyaluronic acid from N-acetylheparosan

Tandem MS can distinguish hyaluronic acid from N-acetylheparosan

Mass spectrometric detection of multiple extended series of neutral highly fucosylated N-acetyllactosamine oligosaccharides in human milk

Glycomics and Mass Spectrometry

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