Multi-charged labeling of oligosaccharides and N-linked glycans
by hexahistidine-based tags for capillary electrophoresis-mass
spectrometry analysis

J 2018

Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis

PARTYKA, Jan; Jana KRENKOVA; Richard CMELIK a František FORET

Základní údaje

Originální název

Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis

Autoři

PARTYKA, Jan; Jana KRENKOVA; Richard CMELIK a František FORET

Vydání

Journal of Chromatography A, Amsterdam, ELSEVIER SCIENCE BV, 2018, 0021-9673

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Full Text

Impakt faktor

Impact factor: 3.858

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/18:00108842

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

Capillary ectrophoresis; Hexahistidine; Labeling; Mass spectrometry; N-linked glycans; Oligosaccharides

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 12. 2019 17:52, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

The labeling by amino acids and peptides was investigated for sensitive and fast analyses of oligosaccharides and N-linked glycans by capillary electrophoresis-mass spectrometry (CE-MS). Peptide tags with a various number of histidine residues were tested for maltooligosaccharide labeling in order to investigate the effect of the size of labels and a number of charges on CE-MS analysis. Nevertheless, the reductive amination labeling of N-linked glycans by a hexahistidine tag resulted in a multiple products formation, therefore a peptide tag was modified by hydrazine functionality in order to perform labeling by hydrazone formation chemistry. This labeling approach significantly improved sensitivity with LOD of labeled maltopentaose determined to be 40 nmol/L and also significantly reduced separation time of neutral maltooligosaccharides and N-linked glycans released from bovine ribonuclease B. Furthermore, the labeling by this multi-cationic peptide hydrazine tag also allowed performing analysis of acidic glycans by CE-MS in a positive ion mode as demonstrated by separation of sialylated N-linked glycans released from bovine fetuin.

Citovat

PARTYKA, Jan; Jana KRENKOVA; Richard CMELIK a František FORET. Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis. Journal of Chromatography A. Amsterdam: ELSEVIER SCIENCE BV, 2018, roč. 1560, JUL, s. 91-96. ISSN 0021-9673. Dostupné z: https://doi.org/10.1016/j.chroma.2018.05.030.

@article{1422236,
   author = {Partyka, Jan and Krenkova, Jana and Cmelik, Richard and Foret, František},
   article_location = {Amsterdam},
   article_number = {JUL},
   doi = {https://doi.org/10.1016/j.chroma.2018.05.030},
   keywords = {Capillary ectrophoresis; Hexahistidine; Labeling; Mass spectrometry; N-linked glycans; Oligosaccharides},
   language = {eng},
   issn = {0021-9673},
   journal = {Journal of Chromatography A},
   title = {Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis},
   url = {https://www.sciencedirect.com/science/article/pii/S0021967318306137},
   volume = {1560},
   year = {2018}
}

TY  - JOUR
ID  - 1422236
AU  - Partyka, Jan - Krenkova, Jana - Cmelik, Richard - Foret, František
PY  - 2018
TI  - Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis
JF  - Journal of Chromatography A
VL  - 1560
IS  - JUL
SP  - 91-96
EP  - 91-96
PB  - ELSEVIER SCIENCE BV
SN  - 00219673
KW  - Capillary ectrophoresis
KW  - Hexahistidine
KW  - Labeling
KW  - Mass spectrometry
KW  - N-linked glycans
KW  - Oligosaccharides
UR  - https://www.sciencedirect.com/science/article/pii/S0021967318306137
L2  - https://www.sciencedirect.com/science/article/pii/S0021967318306137
N2  - The labeling by amino acids and peptides was investigated for sensitive and fast analyses of oligosaccharides and N-linked glycans by capillary electrophoresis-mass spectrometry (CE-MS). Peptide tags with a various number of histidine residues were tested for maltooligosaccharide labeling in order to investigate the effect of the size of labels and a number of charges on CE-MS analysis. Nevertheless, the reductive amination labeling of N-linked glycans by a hexahistidine tag resulted in a multiple products formation, therefore a peptide tag was modified by hydrazine functionality in order to perform labeling by hydrazone formation chemistry. This labeling approach significantly improved sensitivity with LOD of labeled maltopentaose determined to be 40 nmol/L and also significantly reduced separation time of neutral maltooligosaccharides and N-linked glycans released from bovine ribonuclease B. Furthermore, the labeling by this multi-cationic peptide hydrazine tag also allowed performing analysis of acidic glycans by CE-MS in a positive ion mode as demonstrated by separation of sialylated N-linked glycans released from bovine fetuin.
ER  -

PARTYKA, Jan; Jana KRENKOVA; Richard CMELIK a František FORET. Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis. \textit{Journal of Chromatography A}. Amsterdam: ELSEVIER SCIENCE BV, 2018, roč.~1560, JUL, s.~91-96. ISSN~0021-9673. Dostupné z: https://doi.org/10.1016/j.chroma.2018.05.030.

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