131531-80-1Relevant articles and documents
An acceptor analogue of β-1,4-galactosyltransferase: Substrate, inhibitor, or both?
Jiang, Jingqian,Wagner, Gerd K.
, p. 54 - 59 (2017)
Many glycosyltransferase inhibitors in the literature are structurally derived from the donor or acceptor substrate of the respective enzyme. A representative example is 2-naphthyl β-D-GlcNAc, a synthetic GlcNAc glycoside that has been reported as a galactosyltransferase inhibitor. This GlcNAc derivative is attractive as a chemical tool compound for biological and biochemical studies because of its reported potency as an inhibitor, and its short and straightforward synthesis from readily available starting materials. We report that in our hands, 2-naphthyl β-D-GlcNAc behaved, unexpectedly, as an acceptor substrate of the inverting β-1,4-galactosyltransferase (β-1,4-GalT) from bovine milk. This substrate activity has not previously been described. We found that 2-naphthyl β-D-GlcNAc can be an acceptor substrate both for recombinantly expressed β-1,4-GalT, and for a commercial batch of the same enzyme, and both in the presence and absence of bovine serum albumin (BSA). As expected for a full acceptor substrate, this substrate activity was time- and concentration-dependent. Additional experiments show that the observed inhibitor/substrate switch is facilitated by a phosphatase that is an essential component of our enzyme-coupled glycosyltransferase assay. These findings suggest that the behaviour of 2-naphthyl β-D-GlcNAc and related acceptor-based glycosyltransferase inhibitors is strongly dependent on the individual assay conditions. Our results therefore have important implications for the use of 2-naphthyl β-D-GlcNAc and related glycosides as tool compounds in glycobiology and glycobiochemistry.
Design of N-acetyl-6-sulfo-β-D-glucosaminide-based inhibitors of influenza virus sialidase
Sasaki, Kenji,Nishida, Yoshihiro,Kambara, Mikie,Uzawa, Hirotaka,Takahashi, Tadanobu,Suzuki, Takashi,Suzuki, Yasuo,Kobayashi, Kazukiyo
, p. 1367 - 1375 (2007/10/03)
Biological activity of N-acetyl-6-sulfo-β-D-glucosaminides (6-sulfo-GlcNAc 1) having a structural homology to N-acetylneuraminic acid (Neu5Ac 2) and 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (Neu5Ac2en 3) was examined in terms of inhibitory activity against influenza virus sialidase (influenza, A/Memphis/1/71 H3N2). pNP 6-Sulfo-GlcNAc 1a was proved to show substantial activity to inhibit the virus sialidase (IC50=2.8 mM), though p-nitrophenyl (pNP) GlcNAc without 6-sulfo group and pNP 6-sulfo-GlcNH3+ 1b without 2-NHAc showed little activity (IC50 >50 mM). The activity was enhanced nearly 100-fold when the pNP group of 1a was converted to p-acetamidophenyl one 5 (IC50=30 μM) or replaced with 1-naphthyl 6 (IC50=10 μM) or n-propyl one 8 (IC50=11 μM).
Synthesis of N-Acetylmuramyl-L-Alanyl-D-Isoglutamine Aryl β-Glycosides
Zemlyakov,Tsikalov,Kur'yanov,Chirva,Bovin
, p. 390 - 394 (2007/10/03)
Synthesis of N-acetylmuramyl-L-alanyl-D-isoglutamine phenyl and (2-naphthyl) β-glycosides, novel muramyl dipeptide derivatives with phenolic aglycons, was reported. The starting N-acetylglucosamine aryl glycosides were obtained by glycosylation of phenols with peracetylated α-glucosaminyl chloride under the conditions of phase-transfer catalysis and used for the synthesis of 4,6-O-isopropylidene-N-acetylmyramic acid aryl β-glycosides. Condensation of these derivatives with a dipeptide and subsequent deprotection resulted in the intended glycopeptides.
Synthesis of N-Acetylglucosamine Aryl β-Glycosides Catalyzed by Crown Compounds
Kur'yanov,Chupakhina,Zemlyakov,Kotlyar,Kamalov,Chirva
, p. 385 - 389 (2007/10/03)
Glycosylation of various phenols with α-D-glucosaminyl chloride peracetate in a solid phase-liquid system catalyzed by crown compounds was studied. The highest yields of aryl β-glycosides were observed at room temperature in acetonitrile using anhydrous p
Acceptor substrate-based selective inhibition of galactosyltransferases
Chung, Sang J.,Takayama, Shuichi,Wong, Chi-Huey
, p. 3359 - 3364 (2007/10/03)
This paper describes the discovery of glycosyl acceptor analogs as potent and selective inhibitors of α-1,3- and β-1,4- galactosyltransferases. Incorporation of an appropriate aromatic group to the aglycon position of the enzyme's acceptors results in a strong inhibition, representing the first and most potent small uncharged molecules as selective inhibitors of these two enzymes and thus providing a new strategy for the development of selective glycosyltransferase inhibitors.
Stereospecific Synthesis of Aryl β-D-N-Acetylglucopyranosides by Phase Transfer Catalysis
Roy, Rene,Tropper, Francois
, p. 2097 - 2102 (2007/10/02)
Under phase transfer catalyzed conditions, 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-glucopyranosyl chloride (1) reacts with a series of phenoxides to afford high yields of acetylated aryl β-D-N-acetylglucopyranosides (3-8).Deprotection of the hydroxyl g
