Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2011–2012

Harvey, David J.

doi:10.1002/mas.21471

Cited by 36 publications

(29 citation statements)

References 1,685 publications

(685 reference statements)

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“…According to previous studies, direct analysis of native sialylated glycans is difficult, as the negative charge of sialic acid reduces the ionization efficiency in positive-ion mode and the non-derivatized sialic acid residues are often lost due to in- and post source decay [19, 40]. Although negative-ion mode MS is proposed as an alternative option for MALDI analysis of native acidic glycans, it has been demonstrated that the sensitivity of sialylated glycans is at least 10 times less than neutral glycans when using DHB as a matrix [41].…”

Section: Resultsmentioning

confidence: 99%

Carbon Nanoparticles and Graphene Nanosheets as MALDI Matrices in Glycomics: a New Approach to Improve Glycan Profiling in Biological Samples

Banazadeh

Peng

Veillon

et al. 2018

J. Am. Soc. Mass Spectrom.

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Glycomics continues to be a highly dynamic and interesting research area due to the need to comprehensively understand the biological attributes of glycosylation in many important biological functions such as the immune response, cell development, cell differentiation/adhesion, and host-pathogen interactions. Although matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) has proven to be suitable for glycomic profiling studies, there is a need for improved sensitivity in the detection of native glycans, which ionize inefficiently. In this study, we investigated the efficiencies of graphene nanosheets (GNs) and carbon nanoparticles (CNPs) as MALDI matrices and co-matrices in glycan profiling. Our results indicated an enhancement of signal intensity by several orders of magnitude upon using GNs and CNPs in MALDI analysis of N-glycans derived from a variety of biological samples. Interestingly, increasing the amounts of CNPs and GNs improved not only the signal intensities but also prompted in-source decay (ISD) fragmentations, which produced extensive glycosidic and cross-ring cleavages. Our results indicated that the extent of ISD fragmentation could be modulated by CNP and GN concentrations, to obtain MS and pseudo-MS spectra. The results for glycan profiling in high salt solutions confirmed high salt-tolerance capacities for both CNPs and GNs. Finally, the results showed that by using CNPs and GNs as co-matrices, DHB crystal formation was more homogeneous which improved shot-to-shot reproducibility and sensitivity. Graphical Abstract ᅟ.

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Section: Resultsmentioning

confidence: 99%

Carbon Nanoparticles and Graphene Nanosheets as MALDI Matrices in Glycomics: a New Approach to Improve Glycan Profiling in Biological Samples

Banazadeh

Peng

Veillon

et al. 2018

J. Am. Soc. Mass Spectrom.

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“…Various solid and liquid matrices have been reported for enhancing the ion yield of glycans. [9][10][11][12][13][14][15] Another way to improve ionization eciency is to perform derivatization (i.e., labeling). e chemical labeling of the reducing end of glycans was originally developed for HPLC analysis with UV or uorescent detectors.…”

Section: Labeling Of Glycansmentioning

confidence: 99%

“…us, MALDI-MS enjoys widespread use in a variety of applications for the analysis of glycans and glycopeptides. [9][10][11][12][13][14][15] However, the mass spectrometric analysis of glycosylation still remains a challenging task due to the low ionization e ciency, labile nature and complicated branched structures involving various linkage isomers. In general, released glycans show lower ionization e ciency than other biopolymers, such as peptides.…”

Section: Introductionmentioning

confidence: 99%

Sensitive and Structure-Informative <i>N</i>-Glycosylation Analysis by MALDI-MS; Ionization, Fragmentation, and Derivatization

Nishikaze

2017

Mass Spectrometry

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Mass spectrometry (MS) has become an indispensable tool for analyzing post translational modi cations of proteins, including N-glycosylated molecules. Because most glycosylation sites carry a multitude of glycans, referred to as "glycoforms," the purpose of an N-glycosylation analysis is glycoform pro ling and glycosylation site mapping. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has unique characteristics that are suited for the sensitive analysis of N-glycosylated products. However, the analysis is o en hampered by the inherent physico-chemical properties of N-glycans. Glycans are highly hydrophilic in nature, and therefore tend to show low ion yields in both positive-and negative-ion modes.e labile nature and complicated branched structures involving various linkage isomers make structural characterization di cult. is review focuses on MALDI-MS-based approaches for enhancing analytical performance in N-glycosylation research. In particular, the following three topics are emphasized: (1) Labeling for enhancing the ion yields of glycans and glycopeptides, (2) Negative-ion fragmentation for less ambiguous elucidation of the branched structure of N-glycans, (3) Derivatization for the stabilization and linkage isomer discrimination of sialic acid residues.

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“…The analysis of native N-glycans revealed that the O -acetylation pattern was correlated with long-term handling stress, which was most likely to be a product of immune reaction. With the permethylation process, MALDI-MS is the desired technique for profiling glycans28293031. Methylation of all hydroxyl groups of glycans can significantly increase detection sensitivity because the derivatives are considerably more hydrophobic and stable than native glycans.…”

mentioning

confidence: 99%

Characterization of O-acetylation in sialoglycans by MALDI-MS using a combination of methylamidation and permethylation

Zhang

et al. 2017

Sci Rep

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O-Acetylation of sialic acid in protein N-glycans is an important modification and can occur at either 4-, 7-, 8- or 9-position in various combinations. This modification is usually labile under alkaline reaction conditions. Consequently, a permethylation-based analytical method, which has been widely used in glycomics studies, is not suitable for profiling O-acetylation of sialic acids due to the harsh reaction conditions. Alternatively, methylamidation can be used for N-glycan analysis without affecting the base-labile modification of sialic acid. In this report, we applied both permethylation and methylamidation approaches to the analysis of O-acetylation in sialic acids. It has been demonstrated that methylamidation not only stabilizes sialic acids during MALDI processing but also allow for characterization of their O-acetylation pattern. In addition, LC-MS/MS experiments were carried out to distinguish between the O-acetylated glycans with potential isomeric structures. The repeatability of methylamidation was examined to evaluate the applicability of the approach to profiling of O-acetylation in sialic acids. In conclusion, the combination of methylamidation and permethylation methodology is a powerful MALDI-TOF MS-based tool for profiling O-acetylation in sialic acids applicable to screening of N-glycans.

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2011–2012

Cited by 36 publications

References 1,685 publications

Carbon Nanoparticles and Graphene Nanosheets as MALDI Matrices in Glycomics: a New Approach to Improve Glycan Profiling in Biological Samples

Carbon Nanoparticles and Graphene Nanosheets as MALDI Matrices in Glycomics: a New Approach to Improve Glycan Profiling in Biological Samples

Sensitive and Structure-Informative <i>N</i>-Glycosylation Analysis by MALDI-MS; Ionization, Fragmentation, and Derivatization

Characterization of O-acetylation in sialoglycans by MALDI-MS using a combination of methylamidation and permethylation

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