Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
ISSN-L : 0915-7352
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Volume 25, Issue 146
Displaying 1-4 of 4 articles from this issue
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MINIREVIEWS
  • Application of Fluorous Chemistry for Oligosaccharide Synthesis
    Kohtaro Goto, Mamoru Mizuno
    Article type: MINIREVIEW
    2013 Volume 25 Issue 146 Pages 203-213
    Published: 2013
    Released on J-STAGE: November 25, 2013
    DOIhttps://doi.org/10.4052/tigg.25.203
    JOURNAL FREE ACCESS
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    Purification for oligosaccharide synthesis requires an immense amount of time and effort after each synthetic reaction. The fluorous tag method is an efficient synthetic strategy that does not resort column chromatography. Here, we describe oligosaccharide synthesis with the novel fluorous tag. Additionally, we describe how efficiency of oligosaccharide synthesis can be increased by using a combination of the fluorous tag method and other efficient synthetic methodologies.
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  • Glycosylation Regulates CD38 Assembly on the Cell Surface
    Miki Hara-Yokoyama
    Article type: MINIREVIEW
    2013 Volume 25 Issue 146 Pages 215-225
    Published: 2013
    Released on J-STAGE: November 25, 2013
    DOIhttps://doi.org/10.4052/tigg.25.215
    JOURNAL FREE ACCESS
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    The leukocyte cell-surface antigen CD38 is a Type II transmembrane glycoprotein. CD38 is the major NAD+ glycohydrolase in mammals, and it also acts as a raft-dependent signaling molecule to promote cell proliferation or death. Recently, we identified the structural basis for CD38 tetramerization on the cell surface, which underlies the catalytic activity and the localization of CD38 in lipid rafts. The N-linked glycosylation sites are located in strategic positions to prevent further self-association of the tetramer. The glycosylation is likely to ensure the function of CD38, by regulating the cell-surface assembly.
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  • Biomolecular Self-assembling Systems for Multivalent Ligand Display
    Kazunori Matsuura
    Article type: MINIREVIEW
    2013 Volume 25 Issue 146 Pages 227-239
    Published: 2013
    Released on J-STAGE: November 25, 2013
    DOIhttps://doi.org/10.4052/tigg.25.227
    JOURNAL FREE ACCESS
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    Assemblies of multivalent ligands with regular arrangement such as natural glycolipid clusters play important roles in biological molecular recognition. Programmed self-assemblies of DNAs, peptides, and proteins were recently developed as technology to construct artificial nanoassemblies. Molecular systems that display regularly multivalent ligands have been constructed by introducing ligands into the biomolecular nanoassemblies. One-dimensional display of sugars with regular intervals has been achieved by hybridization of glycosylated oligo–DNA with the half-sliding complementary DNA. Three dimensional ligand display by DNA self-assembly has also been possible. On the other hand, ligand display systems on peptide assemblies and viral capsids have also been developed. Virus-like nanocapsules were also constructed by self-assembly of peptides. The present strategies for ligand display can be applied to various biorecognizable materials and drug delivery materials in future.
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