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Synthesis of LacdiNAc-terminated glycoconjugates by mutant galactosyltransferase – A way to new glycodrugs and materials
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SYSNO ASEP 0327139 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Synthesis of LacdiNAc-terminated glycoconjugates by mutant galactosyltransferase – A way to new glycodrugs and materials Author(s) Bojarová, Pavla (MBU-M) ORCID
Křenek, Karel (MBU-M)
Wetjen, K. (DE)
Adamiak, K. (DE)
Pelantová, Helena (MBU-M) ORCID, RID
Bezouška, Karel (MBU-M)
Elling, L. (DE)
Křen, Vladimír (MBU-M) RID, ORCIDSource Title Glycobiology. - : Oxford University Press - ISSN 0959-6658
Roč. 19, č. 5 (2009), s. 509-517Number of pages 9 s. Language eng - English Country US - United States Keywords enzymatic synthesis ; glycomimetics ; glycosyltransferase Subject RIV CE - Biochemistry R&D Projects GP203/09/P024 GA ČR - Czech Science Foundation (CSF) GA204/06/0771 GA ČR - Czech Science Foundation (CSF) OC 136 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000265096000007 DOI 10.1093/glycob/cwp010 Annotation Human placental b1,4-galactosyltransferase-I (EC 2.4.1.38) transfers the galactosyl moiety from UDP-Gal to various GlcNAc or Glc acceptors in vivo. Here, we describe the construction of its Y284L mutant as a His6propeptidecatb4GalT1 construct, in which the Gal-transferase aktivity was totally abolished in favor of its GalNAc-transferase activity. We used this mutant in the synthesis of three monoand bivalent LacdiNAc glycomimetics with good yields. These compounds proved to be powerful ligands of two activation receptors of natural killer cells, NKR-P1 and CD69.A synthetic bivalent tethered di-LacdiNAc is the best currently known precipitation agent for both of these receptors and has promising potential for the development of immunoactive glycodrugs Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2010
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