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

. 2009 May ; 19 (5) : 509-17. [epub] 20090129

Status odvoláno Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic

Typ dokumentu časopisecké články, práce podpořená grantem, odvolaná publikace

Perzistentní odkaz   https://www.medvik.cz/link/pmid19179461

Human placental beta1,4-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-catbeta4GalT1 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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PubMed

Citace poskytuje Crossref.org

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