Počet záznamů: 1
Glycocalix[4]arenes and their affinity to a library of galectins: the linker matters
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SYSNO ASEP 0569335 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Glycocalix[4]arenes and their affinity to a library of galectins: the linker matters Tvůrce(i) Konvalinková, Dorota (MBU-M)
Dolníček, F. (CZ)
Hovorková, Michaela (MBU-M)
Červený, Jakub (MBU-M) ORCID, RID
Kundrát, O. (CZ)
Pelantová, Helena (MBU-M) ORCID, RID
Petrásková, Lucie (MBU-M) ORCID
Cvačka, Josef (UOCHB-X) RID, ORCID
Faizulina, M. (CZ)
Varghese, B. (CZ)
Kovaříček, P. (CZ)
Křen, Vladimír (MBU-M) RID, ORCID
Lhoták, P. (CZ)
Bojarová, Pavla (MBU-M) ORCIDZdroj.dok. Organic & Biomolecular Chemistry. - : Royal Society of Chemistry - ISSN 1477-0520
Roč. 21, č. 6 (2023), s. 1294-1302Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova upper rim ; multivalent ; lectins ; glycoclusters ; recognition ; ligands ; binding ; conformations ; glycoprotein ; selectivity Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology Vědní obor RIV – spolupráce Ústav organické chemie a biochemie - Analytická chemie, separace CEP GA20-00215S GA ČR - Grantová agentura ČR LTC20072 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Omezený přístup Institucionální podpora MBU-M - RVO:61388971 ; UOCHB-X - RVO:61388963 UT WOS 000915472200001 EID SCOPUS 85147721048 DOI 10.1039/d2ob02235d Anotace 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2024 Elektronická adresa https://pubs.rsc.org/en/content/articlelanding/2023/OB/D2OB02235D
Počet záznamů: 1