piperidines and nojirimycin

piperidines has been researched along with nojirimycin* in 2 studies

Other Studies

2 other study(ies) available for piperidines and nojirimycin

ArticleYear
General synthesis and biological evaluation of alpha-1-C-substituted derivatives of fagomine (2-deoxynojirimycin-alpha-C-glycosides).
    Bioorganic & medicinal chemistry, 2005, Mar-15, Volume: 13, Issue:6

    A general synthesis of alpha-1-C-substituted derivatives of fagomine (2-deoxynojirimycin-alpha-C-glycosides) by ring-opening reactions of an aziridine with various heteroatomic nucleophiles, including thiol, amine, alcohol, carboxylate and phosphate, is described. The nine-step reaction sequence proceeded in an overall yield of 14-28% from tri-O-benzyl-D-glucal. Biological evaluation of alpha-1-C-substituted derivatives of fagomine, of the 2-deoxy analog of alpha-homonojirimycin 19 and its 1,N-anhydro derivative 22 as glycosidase inhibitors is reported. The glycosyl phosphate mimetic 15k was found to display no inhibitory activity towards glycogen phosphorylase b and phosphoglucomutase.

    Topics: 1-Deoxynojirimycin; Animals; Aziridines; Cattle; Cyclization; Glucosamine; Glycoside Hydrolases; Glycosides; Humans; Imino Pyranoses; Inhibitory Concentration 50; Molecular Structure; Oxidation-Reduction; Piperidines; Rats; Structure-Activity Relationship

2005
Homonojirimycin and N-methyl-homonojirimycin inhibit N-linked oligosaccharide processing.
    Glycobiology, 1997, Volume: 7, Issue:2

    Homonojirimycin (HNJ) and N-methylhomonojirimycin (MHNJ) were tested as inhibitors of the purified glycoprotein processing enzymes, glucosidase I and glucosidase II. MHNJ was a reasonably good inhibitor of glucosidase I (Ki = 1 x 10(-6) M) and was about three times as effective on this enzyme as was HNJ. On the other hand, HNJ inhibited glucosidase II with a Ki of about 1 x 10(-6) M, whereas MHNJ was three times less effective (Ki = 3 x 10(-5) M). However, the butyl derivative of HNJ had very low activity toward these two processing glucosidases. HNJ and its methyl derivative were also tested in vivo using influenza virus-infected MDCK cells, and measuring the inhibition of N-linked oligosaccharide processing of the viral envelope glycoproteins. With 100 micrograms/ml of MHNJ in the medium, essentially all of the N-linked oligosaccharide chains of the virus were of the "high-mannose" type with the major structure being characterized as Glc3Man9(GlcNAc)2. Similar results were obtained with HNJ although this compound was less effective in vivo as well as in vitro. These results are in keeping with these inhibitors being effective at the glucosidase I step. Both inhibitors were also tested in MDCK cell cultures to determine whether they affected the in vivo synthesis of proteins, or of lipid-linked saccharides. In contrast to deoxynojirimycin, which has been reported to inhibit the formation of lipid-linked saccharides, no effects were seen on either the incorporation of mannose into lipid-linked saccharides or the incorporation of leucine into protein.

    Topics: 1-Deoxynojirimycin; alpha-Glucosidases; Cells, Cultured; Dose-Response Relationship, Drug; Enzyme Inhibitors; Glucosamine; Glycoproteins; Glycoside Hydrolase Inhibitors; Imino Pyranoses; Oligosaccharides; Orthomyxoviridae; Piperidines; Protein Processing, Post-Translational; Viral Envelope Proteins

1997