Glycocalix[4]arenes and their affinity to a library of galectins: the linker matters

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00569335" target="_blank" >RIV/61388963:_____/23:00569335 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/23:00569335 RIV/60461373:22310/23:43927868 RIV/68407700:21460/23:00365020 RIV/00216208:11310/23:10458206

Výsledek na webu

<a href="https://pubs.rsc.org/en/content/articlelanding/2023/OB/D2OB02235D" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2023/OB/D2OB02235D</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/d2ob02235d" target="_blank" >10.1039/d2ob02235d</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Glycocalix[4]arenes and their affinity to a library of galectins: the linker matters

Popis výsledku v původním jazyce

Galectins are lectins that bind beta-galactosides. They are involved in important extra- and intracellular biological processes such as apoptosis, and regulation of the immune system or the cell cycle. High-affinity ligands of galectins may introduce new therapeutic approaches or become new tools for biomedical research. One way of increasing the low affinity of beta-galactoside ligands to galectins is their multivalent presentation, e.g., using calixarenes. We report on the synthesis of glycocalix[4]arenes in cone, partial cone, 1,2-alternate, and 1,3-alternate conformations carrying a lactosyl ligand on three different linkers. The affinity of the prepared compounds to a library of human galectins was determined using competitive ELISA assay and biolayer interferometry. Structure-affinity relationships regarding the influence of the linker and the core structure were formulated. Substantial differences were found between various linker lengths and the position of the triazole unit. The formation of supramolecular clusters was detected by atomic force microscopy. The present work gives a systematic insight into prospective galectin ligands based on the calix[4]arene core.

Název v anglickém jazyce

Glycocalix[4]arenes and their affinity to a library of galectins: the linker matters

Popis výsledku anglicky

Galectins are lectins that bind beta-galactosides. They are involved in important extra- and intracellular biological processes such as apoptosis, and regulation of the immune system or the cell cycle. High-affinity ligands of galectins may introduce new therapeutic approaches or become new tools for biomedical research. One way of increasing the low affinity of beta-galactoside ligands to galectins is their multivalent presentation, e.g., using calixarenes. We report on the synthesis of glycocalix[4]arenes in cone, partial cone, 1,2-alternate, and 1,3-alternate conformations carrying a lactosyl ligand on three different linkers. The affinity of the prepared compounds to a library of human galectins was determined using competitive ELISA assay and biolayer interferometry. Structure-affinity relationships regarding the influence of the linker and the core structure were formulated. Substantial differences were found between various linker lengths and the position of the triazole unit. The formation of supramolecular clusters was detected by atomic force microscopy. The present work gives a systematic insight into prospective galectin ligands based on the calix[4]arene core.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

Organic & Biomolecular Chemistry

ISSN

1477-0520

e-ISSN

1477-0539

Svazek periodika

21

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

1294-1302

Kód UT WoS článku

000915472200001

EID výsledku v databázi Scopus

2-s2.0-85147721048