All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GC15-02578J" target="_blank" >GC15-02578J: Modified multivalent poly-N-acetyllactosamine glycans as novel ligands of human galectin-3</a><br>

  • Continuities

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

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Advanced Synthesis & Catalysis

  • ISSN

    1615-4150

  • e-ISSN

  • Volume of the periodical

    359

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    8

  • Pages from-to

    2101-2108

  • UT code for WoS article

    000403567500009

  • EID of the result in the Scopus database

    2-s2.0-85020844834