Journal
GLYCOBIOLOGY
Volume 19, Issue 5, Pages 509-517Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwp010
Keywords
enzymatic synthesis; glycomimetics; glycosyltransferase; LacdiNAc; natural killer cell
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Funding
- The Czech National Science Foundation [203/09/P024, 204/06/0771]
- Czech Ministry of Education [COST D34, CM0701 chemistry actions (OC 136, LC06010), MSM0021620808]
- Deutsche Forschungsgemeinschaft [EL 135/6-1, EL 135/6-2, EL 135/8-1, EL 135/10-1]
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Human placental beta 1,4-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 His(6)propeptide-cat beta 4GalT1 construct, in which the Gal-transferase activity was totally abolished in favor of its GalNAc-transferase activity. We used this mutant in the synthesis of three mono- and 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.
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