Synthesis of LacdiNAc-terminated glycoconjugates by mutant galactosyltransferase – A way to new glycodrugs and materials

0327139 - MBÚ 2010 RIV US eng J - Článek v odborném periodiku
Bojarová, Pavla - Křenek, Karel - Wetjen, K. - Adamiak, K. - Pelantová, Helena - Bezouška, Karel - Elling, L. - Křen, Vladimír
Synthesis of LacdiNAc-terminated glycoconjugates by mutant galactosyltransferase – A way to new glycodrugs and materials.
Glycobiology. Roč. 19, č. 5 (2009), s. 509-517. ISSN 0959-6658. E-ISSN 1460-2423
Grant CEP: GA ČR GP203/09/P024; GA ČR GA204/06/0771; GA MŠMT OC 136; GA MŠMT(CZ) LC06010
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: enzymatic synthesis * glycomimetics * glycosyltransferase
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.929, rok: 2009

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
Trvalý link: http://hdl.handle.net/11104/0174037