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Systematic syntheses and inhibitory activities of bisubstrate-type inhibitors of sialyltransferases

  • Hiroshi Hinou
  • , Xue Sun
  • , Yukishige Ito
  • Inst. of Phys. and Chem. Research
  • Nihon University
  • Emory University School of Medicine

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Bisubstrate-type sialyltransferase inhibitors 1/2a-e, having CMP-NeuAc and N-acetyllactosamine (or lactose) moieties connected by an alkanedithiol linker, were synthesized systematically. A uniform synthetic strategy was adopted that consists of consecutive couplings of three components (N-acetyllactosamine or lactose, sialic acid, and CMP), followed by oxidation. Due to the sensitivity of the compounds under alkaline conditions, final deprotection required careful monitoring by 1H NMR. The inhibitory activities of 1/2a-e toward ST6N and ST3N indicated that both the structure of the acceptor moiety and the distance between donor and acceptor moieties were important.
Original languageEnglish
Pages (from-to)5602-5613
Number of pages12
JournalJournal of Organic Chemistry
Volume68
Issue number14
DOIs
StatePublished - Jul 11 2003

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