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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F18%3A00108842" target="_blank" >RIV/00216224:14310/18:00108842 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081715:_____/18:00489967

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0021967318306137" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0021967318306137</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.chroma.2018.05.030" target="_blank" >10.1016/j.chroma.2018.05.030</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Chromatography A

ISSN

0021-9673

e-ISSN

1873-3778

Svazek periodika

1560

Číslo periodika v rámci svazku

JUL

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

91-96

Kód UT WoS článku

000434902900012

EID výsledku v databázi Scopus

2-s2.0-85046873722