Two-Step Enzymatic Synthesis of beta-D-N-Acetylgalactosamine-(1 -> 4)-D-N-acetylglucosamine (LacdiNAc) Chitooligomers for Deciphering Galectin Binding Behavior

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00476013" target="_blank" >RIV/61388971:_____/17:00476013 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/adsc.201700331" target="_blank" >http://dx.doi.org/10.1002/adsc.201700331</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/adsc.201700331" target="_blank" >10.1002/adsc.201700331</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Two-Step Enzymatic Synthesis of beta-D-N-Acetylgalactosamine-(1 -> 4)-D-N-acetylglucosamine (LacdiNAc) Chitooligomers for Deciphering Galectin Binding Behavior

Popis výsledku v původním jazyce

A two-step synthesis of engineered variants of Talaromyces flavus Beta-N-acetylhexosaminidase (TfHexY470N) and human beta4-galactosyltransferase (beta4GalTY284L) yielded complex glycans comprising a chitooligomeric spacer (beta1,4GlcNAc)n=0-3 terminated with a beta4-linked beta-d-N-acetylgalactosamine-(1-4)-d-N-acetylglucosamine (LacdiNAc) epitope. These compounds are novel inhibitors of human galectin-3 (Gal-3), a widely spread animal lectin with important physiological functions in cellular communication. The multivalent presentation of glycan oligomers was accomplished by chemical conjugation of glycans to lysine residues of bovine serum albumin (BSA). Binding studies of Gal-3 to immobilized BSA neo-glycoconjugates revealed the beneficial influence of the chitooligomeric spacer for the ligand-lectin affinity. We conclude that the use of the (beta1,4GlcNAc)n=0–3 spacer is a perfect nature-like solution for the presentation of elaborated Gal-3 glycan epitopes that surpasses the performance of commonly used synthetic spacers.

Název v anglickém jazyce

Two-Step Enzymatic Synthesis of beta-D-N-Acetylgalactosamine-(1 -> 4)-D-N-acetylglucosamine (LacdiNAc) Chitooligomers for Deciphering Galectin Binding Behavior

Popis výsledku anglicky

A two-step synthesis of engineered variants of Talaromyces flavus Beta-N-acetylhexosaminidase (TfHexY470N) and human beta4-galactosyltransferase (beta4GalTY284L) yielded complex glycans comprising a chitooligomeric spacer (beta1,4GlcNAc)n=0-3 terminated with a beta4-linked beta-d-N-acetylgalactosamine-(1-4)-d-N-acetylglucosamine (LacdiNAc) epitope. These compounds are novel inhibitors of human galectin-3 (Gal-3), a widely spread animal lectin with important physiological functions in cellular communication. The multivalent presentation of glycan oligomers was accomplished by chemical conjugation of glycans to lysine residues of bovine serum albumin (BSA). Binding studies of Gal-3 to immobilized BSA neo-glycoconjugates revealed the beneficial influence of the chitooligomeric spacer for the ligand-lectin affinity. We conclude that the use of the (beta1,4GlcNAc)n=0–3 spacer is a perfect nature-like solution for the presentation of elaborated Gal-3 glycan epitopes that surpasses the performance of commonly used synthetic spacers.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GC15-02578J" target="_blank" >GC15-02578J: Modifikované multivalentní poly-N-acetyllaktosaminové glykany jako nové ligandy pro lidský galektin-3</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Advanced Synthesis & Catalysis

ISSN

1615-4150

e-ISSN

—

Svazek periodika

359

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

2101-2108

Kód UT WoS článku

000403567500009

EID výsledku v databázi Scopus

2-s2.0-85020844834