Selective enrichment of sialylated glycopeptides with a <scp>d</scp>-allose@SiO<sub>2</sub> matrix

Sun, Na; Xiong, Yüting; Qing, Guangyan; Zhao, Yan‐Xia; Li, Xiuling; Liang, Xinmiao

doi:10.1039/c8ra07192f

Cited by 11 publications

(6 citation statements)

References 34 publications

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“…In another study, identical results were obtained with Sepharose, PGC and dextran‐bonded silica for the separation of complex N ‐glycans (Chen, Ding, et al, 2018). Sun, Xiong, et al (2018) have developed a D‐allose@SiO 2 matrix and found that enrichment of sialylated glycopeptides was notably higher than with the commercially available Sepharose CL‐6B or TiO 2 resins.…”

Section: Studies On Specific Carbohydrate Typesmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018

Harvey

2021

Mass Spectrometry Reviews

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This review is the tenth update of the original article published in 1999 on the application of matrix‐assisted laser desorption/ionization mass spectrometry (MALDI) mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2018. Also included are papers that describe methods appropriate to glycan and glycoprotein analysis by MALDI, such as sample preparation techniques, even though the ionization method is not MALDI. Topics covered in the first part of the review include general aspects such as theory of the MALDI process, new methods, matrices, derivatization, MALDI imaging, fragmentation and the use of arrays. The second part of the review is devoted to applications to various structural types such as oligo‐ and poly‐saccharides, glycoproteins, glycolipids, glycosides, and biopharmaceuticals. Most of the applications are presented in tabular form. The third part of the review covers medical and industrial applications of the technique, studies of enzyme reactions, and applications to chemical synthesis. The reported work shows increasing use of combined new techniques such as ion mobility and highlights the impact that MALDI imaging is having across a range of diciplines. MALDI is still an ideal technique for carbohydrate analysis and advancements in the technique and the range of applications continue steady progress.

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Section: Studies On Specific Carbohydrate Typesmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018

Harvey

2021

Mass Spectrometry Reviews

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“…Glycopeptide enrichment of tryptic digested fetuin and BSA (the molar ratio of fetuin to BSA is 1:100) using TiO 2 was performed according to the reported method [11,22,37].…”

Section: Enrichment Of Glycopeptides With Tiomentioning

confidence: 99%

“…The nonglycopeptides were not labeled in the mass spectra of a and c glycosylation groups of identified glycopeptides is presented in Table S1 (see ESM). For comparison, the commercial TiO 2 beads, which have also been used in the enrichment of SGPs via a multipoint binding, similar to a multidentate binding, between negatively charged sialic acid and TiO 2 [11,42], were employed to enrich glycopeptides from the mixtures of fetuin and BSA according to the reported extraction method [11,22,37]. As shown in Fig.…”

Section: Enrichment Performance Of Mpmf Materials To Sgpsmentioning

confidence: 99%

Selective enrichment of sialylated glycopeptides with mesoporous poly-melamine-formaldehyde (mPMF) material

et al. 2020

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Analysis of glycoprotein sialylation is challenging due to the relatively low abundance of sialylated glycopeptides (SGPs) in complex biosamples and low signals of SGPs in mass spectrometry. In this study, a mesoporous poly-melamine-formaldehyde (mPMF) polymer was prepared and utilized as the high-efficiency sorbent for SGPs. The mPMF polymer featured high surface area (755.4 m 2 g −1 ) and high density of amine and triazine functional groups. This polymer demonstrated high enrichment selectivity (resistant to 100 molar fold interference of BSA) and superior adsorption capacity (560 mg g −1 ) for SGPs. The high performance of mPMF toward SGPs ascribes to the unique physicochemical properties of mPMF and high density of accessible binding sites for glycopeptides. Further application of mPMF to HeLa S3 cell lysate resulted in 576 characterized glycopeptides with 218 unique glycosylation sites. This finding provides a new choice of promising extraction approach for characterization of protein glycosylation.

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“…Although exhibiting high SGP enrichment selectivity, hydrazide chemistry-based methods lose the information of terminal SAs . Recently, various novel solid-phase materials have been developed to enrich SGPs exclusively, on account of in-depth interdisciplinarity and a joint force of materials science and analytical chemistry to solve problems. − Among them, an interesting study demonstrated the unique advantage of dynamic covalent chemistry based on Schiff-base hydrolysis in capturing SGPs . Despite the excellent performance, the uniqueness of each material and complicated process for producing as well as characterizing them hindered their widespread applications in general analytical labs.…”

Section: Introductionmentioning

confidence: 99%

Selective Enrichment of Sialylglycopeptides Enabled by Click Chemistry and Dynamic Covalent Exchange

Huang

et al. 2022

Anal. Chem.

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Despite the important roles of protein sialylation in biological processes such as cellular interaction and cancer progression, simple and effective methods for the analysis of intact sialylglycopeptides (SGPs) are still limited. Analyses of low-abundance SGPs typically require efficient enrichment prior to comprehensive liquid chromatography–mass spectrometry (LC–MS)-based analysis. Here, a novel workflow combining mild periodate oxidation, hydrazide chemistry, copper-catalyzed azide/alkyne cycloaddition (CuAAC) click chemistry, and dynamic covalent exchange has been developed for selective enrichment of SGPs. The intact SGPs could be separated easily from protein tryptic digests, and the signature ions were produced during LC–MS/MS for unambiguous identification. The structure of the signature ions and corresponding dynamic covalent exchange were confirmed by using an isotopic reagent. Under the optimized condition, over 70% enrichment efficiency of SGPs was achieved using bovine fetuin digests, and the method was successfully applied to complex biological samples, such as a mouse lung tissue extract. The high enrichment efficiency, good reproducibility, and easily adopted procedure without the need to generate specialized materials make this method a promising tool for broad applications in SGP analysis.

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Selective enrichment of sialylated glycopeptides with a d-allose@SiO₂ matrix

Abstract: Abnormal sialylation of glycoprotein is associated with different kinds of cancers and neurodegenerative diseases.

Cited by 11 publications

References 34 publications

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018

Selective enrichment of sialylated glycopeptides with mesoporous poly-melamine-formaldehyde (mPMF) material

Selective Enrichment of Sialylglycopeptides Enabled by Click Chemistry and Dynamic Covalent Exchange

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Selective enrichment of sialylated glycopeptides with a d-allose@SiO2 matrix

Abstract: Abnormal sialylation of glycoprotein is associated with different kinds of cancers and neurodegenerative diseases.

Cited by 11 publications

References 34 publications

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018

Selective enrichment of sialylated glycopeptides with mesoporous poly-melamine-formaldehyde (mPMF) material

Selective Enrichment of Sialylglycopeptides Enabled by Click Chemistry and Dynamic Covalent Exchange

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Selective enrichment of sialylated glycopeptides with a d-allose@SiO₂ matrix