Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry

Abstract Sialylation is a glycosylation feature that occurs in different linkages at the non-reducing end of a glycan moiety, the linkage isomers are often differentially associated with various biological processes. Due to very similar physico-chemical properties, the separation of isomeric sialyla...

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Autores principales:	Guinevere S. M. Kammeijer, Bas C. Jansen, Isabelle Kohler, Anthonius A. M. Heemskerk, Oleg A. Mayboroda, Paul J. Hensbergen, Julie Schappler, Manfred Wuhrer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9b6a700734e940f1ad472f01a77e63ea
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spelling	oai:doaj.org-article:9b6a700734e940f1ad472f01a77e63ea2021-12-02T16:07:02ZSialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry10.1038/s41598-017-03838-y2045-2322https://doaj.org/article/9b6a700734e940f1ad472f01a77e63ea2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03838-yhttps://doaj.org/toc/2045-2322Abstract Sialylation is a glycosylation feature that occurs in different linkages at the non-reducing end of a glycan moiety, the linkage isomers are often differentially associated with various biological processes. Due to very similar physico-chemical properties, the separation of isomeric sialylated glycopeptides remains challenging but of utmost importance in the biomedicine and biotechnology, including biomarker discovery, glyco-engineering and biopharmaceutical characterization. This study presents the implementation of a high-resolution separation platform based on capillary electrophoresis – mass spectrometry (CE–MS) allowing for the selective analysis of α2,3- and α2,6-sialylated glycopeptides. These differentially linked glycopeptides showed an identical fragmentation pattern (collision induced dissociation) but different electrophoretic mobilities, allowing for baseline separation of the different linkages without the need for an extensive sample preparation. The different migration behavior between the two moieties was found to correlate with differences in pKa values. Using a novel methodology adapted from the so-called internal standard CE approach, a relative difference of 3.4·10−2 in pKa unit was determined. This approach was applied for the analysis of tryptic glycopeptides of prostate specific antigen, which shows highly complex and heterogeneous glycosylation. The developed platform therefore appears attractive for the identification of differentially linked sialic acids that may be related to pathological conditions.Guinevere S. M. KammeijerBas C. JansenIsabelle KohlerAnthonius A. M. HeemskerkOleg A. MayborodaPaul J. HensbergenJulie SchapplerManfred WuhrerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Guinevere S. M. Kammeijer Bas C. Jansen Isabelle Kohler Anthonius A. M. Heemskerk Oleg A. Mayboroda Paul J. Hensbergen Julie Schappler Manfred Wuhrer Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
description	Abstract Sialylation is a glycosylation feature that occurs in different linkages at the non-reducing end of a glycan moiety, the linkage isomers are often differentially associated with various biological processes. Due to very similar physico-chemical properties, the separation of isomeric sialylated glycopeptides remains challenging but of utmost importance in the biomedicine and biotechnology, including biomarker discovery, glyco-engineering and biopharmaceutical characterization. This study presents the implementation of a high-resolution separation platform based on capillary electrophoresis – mass spectrometry (CE–MS) allowing for the selective analysis of α2,3- and α2,6-sialylated glycopeptides. These differentially linked glycopeptides showed an identical fragmentation pattern (collision induced dissociation) but different electrophoretic mobilities, allowing for baseline separation of the different linkages without the need for an extensive sample preparation. The different migration behavior between the two moieties was found to correlate with differences in pKa values. Using a novel methodology adapted from the so-called internal standard CE approach, a relative difference of 3.4·10−2 in pKa unit was determined. This approach was applied for the analysis of tryptic glycopeptides of prostate specific antigen, which shows highly complex and heterogeneous glycosylation. The developed platform therefore appears attractive for the identification of differentially linked sialic acids that may be related to pathological conditions.
format	article
author	Guinevere S. M. Kammeijer Bas C. Jansen Isabelle Kohler Anthonius A. M. Heemskerk Oleg A. Mayboroda Paul J. Hensbergen Julie Schappler Manfred Wuhrer
author_facet	Guinevere S. M. Kammeijer Bas C. Jansen Isabelle Kohler Anthonius A. M. Heemskerk Oleg A. Mayboroda Paul J. Hensbergen Julie Schappler Manfred Wuhrer
author_sort	Guinevere S. M. Kammeijer
title	Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
title_short	Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
title_full	Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
title_fullStr	Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
title_full_unstemmed	Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
title_sort	sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9b6a700734e940f1ad472f01a77e63ea
work_keys_str_mv	AT guineveresmkammeijer sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT bascjansen sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT isabellekohler sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT anthoniusamheemskerk sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT olegamayboroda sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT pauljhensbergen sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT julieschappler sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry AT manfredwuhrer sialicacidlinkagedifferentiationofglycopeptidesusingcapillaryelectrophoresiselectrosprayionizationmassspectrometry
_version_	1718384792768086016

Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry

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