Recent Developments in Liquid Chromatography and Capillary Electrophoresis for the Analysis of Glycoprotein Glycans

Suzuki, Shigeo

doi:10.2116/analsci.29.1117

Cited by 26 publications

(7 citation statements)

References 178 publications

(162 reference statements)

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“…Owing to its capacity to resolve complex proteomics samples, high compatibility with MS detection, and readily available automation system, liquid chromatography (LC) is the separation method of choice when coupled to mass spectrometers to analyze glycopeptides (21). Offline LC fractionation of glycopeptides is a feasible approach for achieving a certain amount of separation, whereas online LC-MS analysis is more routinely adopted in glycoproteomics.…”

Section: Analytical Separation Of Glycopeptidesmentioning

confidence: 99%

Carbohydrates on Proteins: Site-Specific Glycosylation Analysis by Mass Spectrometry

Zhu

Desaire²

2015

Annual Rev. Anal. Chem.

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Glycosylation on proteins adds complexity and versatility to these biologically vital macromolecules. To unveil the structure-function relationship of glycoproteins, glycopeptide-centric analysis using mass spectrometry (MS) has become a method of choice because the glycan is preserved on the glycosylation site and site-specific glycosylation profiles of proteins can be readily determined. However, glycopeptide analysis is still challenging given that glycopeptides are usually low in abundance and relatively difficult to detect and the resulting data require expertise to analyze. Viewing the urgent need to address these challenges, emerging methods and techniques are being developed with the goal of analyzing glycopeptides in a sensitive, comprehensive, and high-throughput manner. In this review, we discuss recent advances in glycoprotein and glycopeptide analysis, with topics covering sample preparation, analytical separation, MS and tandem MS techniques, as well as data interpretation and automation.

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Section: Analytical Separation Of Glycopeptidesmentioning

confidence: 99%

Carbohydrates on Proteins: Site-Specific Glycosylation Analysis by Mass Spectrometry

Zhu

Desaire²

2015

Annual Rev. Anal. Chem.

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“…There are several excellent reviews focusing on the glycosylation analysis of therapeutic glycoproteins in detail [58][59][60][61][62][63]. N-glycosylation analysis of therapeutic proteins can be performed at three different levels (intact protein, glycopeptide, and released glycans), as depicted in Figure 3 [64].…”

Section: Analytical Methods To Track N-glycosylation Patternsmentioning

confidence: 99%

The glycosylation aspects of biosimilarity

Guttman¹

2018

J Bioanal Biomed

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Teaser: This review summarizes the critical quality attributes of biosimilarity, also introducing the glycosimilarity index as an additional parameter to prove similarity between innovator and biosimilar products. Highlights The critical quality attributes of biosimilarity are reviewed  Regulatory and statistical considerations are summarized.  Importance of glycosylation analysis during biosimilar production is detailed.  Analytical methods to track N-glycosylation patterns are reviewed.  Glycosimilarity index is introduced.The recent expiration of several protein therapeutics opened the door for biosimilar development. Biosimilars are biologic medical products that are similar but not identical copies of already-authorized protein therapeutics. Critical quality attributes (CQA), such as post-translational modifications of recombinant biotherapeutics, are important for the clinical efficacy and safety of both the innovative biologics and their biosimilar counterparts. Here, we summarize biosimilarity CQAs, considering the regulatory guidelines and the statistical aspects (e.g., biosimilarity index) and then discuss glycosylation as one of the important attributes of biosimilarity. Finally, we introduced the 'Glycosimilarity Index', which is based on the averaged biosimilarity criterion.

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“…Mechref, Hu, Desantos-Garcia, Hussein, & Tang, 2013; S. Suzuki, 2013; Zamfir & Peter-Katalinic, 2004).…”

Section: 3 Quantitative Glycomics Platformsmentioning

confidence: 99%

Quantitative Glycomics

Veillon

Zhou

Mechref

2017

Methods in Enzymology

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Glycosylation is one of the most common and essential protein modifications. Glycans conjugated to biomolecules modulate the function of such molecules through both direct recognition of glycan structures and indirect mechanisms that involve the control of protein turnover rates, stability, and conformation. The biological attributes of glycans in numerous biological processes and implications in a number of diseases highlight the necessity for comprehensive characterization of protein glycosylation. This chapter review cutting-edge-methods and tools developed to facilitated quantitative glycomics. The chapter highlight the different methods employed for the release and purification of glycans from biological samples. The most effective labeling methods developed for sensitive quantitative glycomics are also described and discussed. The chromatographic approaches that have been used effectively in glycomics are also highlighted.

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Recent Developments in Liquid Chromatography and Capillary Electrophoresis for the Analysis of Glycoprotein Glycans

Cited by 26 publications

References 178 publications

Carbohydrates on Proteins: Site-Specific Glycosylation Analysis by Mass Spectrometry

Carbohydrates on Proteins: Site-Specific Glycosylation Analysis by Mass Spectrometry

The glycosylation aspects of biosimilarity

Quantitative Glycomics

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