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Glycan analysis of therapeutic glycoproteins

Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell systems. The glycan moieties attached to the proteins can directly affect protein stability, bioactivity, and immunogenicity. Therefore, glycan variants of a glycoprotein product must be adequately analyzed and contro...

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Detalles Bibliográficos
Autores principales: Zhang, Lei, Luo, Shen, Zhang, Baolin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966609/
https://www.ncbi.nlm.nih.gov/pubmed/26599345
http://dx.doi.org/10.1080/19420862.2015.1117719
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author Zhang, Lei
Luo, Shen
Zhang, Baolin
author_facet Zhang, Lei
Luo, Shen
Zhang, Baolin
author_sort Zhang, Lei
collection PubMed
description Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell systems. The glycan moieties attached to the proteins can directly affect protein stability, bioactivity, and immunogenicity. Therefore, glycan variants of a glycoprotein product must be adequately analyzed and controlled to ensure product quality. However, the inherent complexity of protein glycosylation poses a daunting analytical challenge. This review provides an update of recent advances in glycan analysis, including the potential utility of lectin-based microarray for high throughput glycan profiling. Emphasis is placed on comparison of the major types of analytics for use in determining unique glycan features such as glycosylation site, glycan structure, and content.
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spelling pubmed-49666092016-08-24 Glycan analysis of therapeutic glycoproteins Zhang, Lei Luo, Shen Zhang, Baolin MAbs Review Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell systems. The glycan moieties attached to the proteins can directly affect protein stability, bioactivity, and immunogenicity. Therefore, glycan variants of a glycoprotein product must be adequately analyzed and controlled to ensure product quality. However, the inherent complexity of protein glycosylation poses a daunting analytical challenge. This review provides an update of recent advances in glycan analysis, including the potential utility of lectin-based microarray for high throughput glycan profiling. Emphasis is placed on comparison of the major types of analytics for use in determining unique glycan features such as glycosylation site, glycan structure, and content. Taylor & Francis 2015-11-24 /pmc/articles/PMC4966609/ /pubmed/26599345 http://dx.doi.org/10.1080/19420862.2015.1117719 Text en This article not subject to US copyright law. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Review
Zhang, Lei
Luo, Shen
Zhang, Baolin
Glycan analysis of therapeutic glycoproteins
title Glycan analysis of therapeutic glycoproteins
title_full Glycan analysis of therapeutic glycoproteins
title_fullStr Glycan analysis of therapeutic glycoproteins
title_full_unstemmed Glycan analysis of therapeutic glycoproteins
title_short Glycan analysis of therapeutic glycoproteins
title_sort glycan analysis of therapeutic glycoproteins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966609/
https://www.ncbi.nlm.nih.gov/pubmed/26599345
http://dx.doi.org/10.1080/19420862.2015.1117719
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