Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals

The specific glycosylation patterns of biological drugs often impact the efficacy and safety of the therapeutic product. Here the authors describe a native mass spectrometry approach that allows the resolution of highly complex glycosylation patterns on large proteins, which they apply to the therap...

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Autores principales:	Therese Wohlschlager, Kai Scheffler, Ines C. Forstenlehner, Wolfgang Skala, Stefan Senn, Eugen Damoc, Johann Holzmann, Christian G. Huber
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/652a3252f9884ca095fe82ff547d3b84
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spelling	oai:doaj.org-article:652a3252f9884ca095fe82ff547d3b842021-12-02T14:40:03ZNative mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals10.1038/s41467-018-04061-72041-1723https://doaj.org/article/652a3252f9884ca095fe82ff547d3b842018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04061-7https://doaj.org/toc/2041-1723The specific glycosylation patterns of biological drugs often impact the efficacy and safety of the therapeutic product. Here the authors describe a native mass spectrometry approach that allows the resolution of highly complex glycosylation patterns on large proteins, which they apply to the therapeutic Fc-fusion protein Etanercept.Therese WohlschlagerKai SchefflerInes C. ForstenlehnerWolfgang SkalaStefan SennEugen DamocJohann HolzmannChristian G. HuberNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Therese Wohlschlager Kai Scheffler Ines C. Forstenlehner Wolfgang Skala Stefan Senn Eugen Damoc Johann Holzmann Christian G. Huber Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
description	The specific glycosylation patterns of biological drugs often impact the efficacy and safety of the therapeutic product. Here the authors describe a native mass spectrometry approach that allows the resolution of highly complex glycosylation patterns on large proteins, which they apply to the therapeutic Fc-fusion protein Etanercept.
format	article
author	Therese Wohlschlager Kai Scheffler Ines C. Forstenlehner Wolfgang Skala Stefan Senn Eugen Damoc Johann Holzmann Christian G. Huber
author_facet	Therese Wohlschlager Kai Scheffler Ines C. Forstenlehner Wolfgang Skala Stefan Senn Eugen Damoc Johann Holzmann Christian G. Huber
author_sort	Therese Wohlschlager
title	Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
title_short	Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
title_full	Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
title_fullStr	Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
title_full_unstemmed	Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
title_sort	native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/652a3252f9884ca095fe82ff547d3b84
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Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals

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