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  • (iso-branched) C17 sphingoid-bases  (1)
  • Cell-cell interaction  (1)
  • Springer  (2)
  • Würzburg : Freunde der Würzburger Geowissenschaften
  • 2000-2004
  • 1995-1999  (2)
Collection
Keywords
Publisher
  • Springer  (2)
  • Würzburg : Freunde der Würzburger Geowissenschaften
Years
  • 2000-2004
  • 1995-1999  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Structural analysis of neutral glycosphingolipids from Ascaris suum adults (Nematoda: Ascaridida) (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 389-399 
    Details
    ISSN: 1573-4986
    Keywords: arthro-series glycosphingolipids ; Ascaris suum ; (iso-branched) C17 sphingoid-bases ; neutral glycosphingolipids ; parasitic nematodes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The neutral glycosphingolipid fraction from adults of the pig parasitic nematode, Ascaris suum, was resolved into four components on thin-layer chromatography. The high-performance liquid chromatography-isolated components were structurally analysed by: methylation analysis; exoglycosidase cleavage; gas-liquid chromatography/mass spectrometry; liquid secondary-ion mass spectrometry; and, in particular, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Their chemical structures were determined as: Glc(β1-1)ceramide, Man(β1-4)Glc(β1-1)ceramide, GlcNAc(β1-3)Man(β1-4)Glc(β1-1)ceramide and Gal(α1-3)GalNAc(β1-4)GlcNAc(β1-3)Man(β1-4)Glc(β1-1)ceramide; and were characterized as belonging to the arthro-series of protostomial glycosphingolipids. No glycosphingolipid component corresponding to ceramide tetrasaccharide was detected during these analyses. The ceramide composition of the parent glycosphingolipids was dominated by the 2-(R)-hydroxy C24:0 fatty acid, cerebronic acid, and C17 sphingoid-bases: 15-methylhexadecasphing-4-enine and 15-methylhexadecaphinganine in approximately equal proportions. The component ceramide monohexoside was characterized by an additional 15-methylhexadecaphytosphingosine. Abbreviations: CDH, ceramide dihexoside; Cer, ceramide; CMH, ceramide monohexoside; CPH, ceramide pentahexoside; CTH, ceramide trihexoside; CTetH, ceramide tetrahexoside; Hex, hexose; HexNAc, N-acetylhexosamine; HPTLC, high-performance thin-layer chromatography; LSIMS, liquid secondary-ion mass spectrometry; MALDI-TOF-MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; N-, Nz- and A-glyco(sphingo)lipids, neutral, neutralzwitterionic and acidic glyco(sphingo)lipids, respectively
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018530914067
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Design of superactive and selective integrin receptor antagonists containing the RGD sequence (1995)
    Springer
    International journal of peptide research and therapeutics 2 (1995), S. 155-160 
    Details
    ISSN: 1573-3904
    Keywords: Cell-cell interaction ; Inhibition ; Rational design of spatial structures ; β-Turn mimetics ; Peptidomimetics ; Retro-inverso peptides ; Sugar amino acids in cyclic peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Integrins play a major role in cell-cell and cell-matrix interactions. The majority of the different types of integrins recognize the tripeptide sequence arginine-glycine-aspartic acid (RGD). To explore the spatial requirements of the pharmacophore for receptor selectivity and high activity, a new procedure, ‘spatial screening’, was used. The procedure is based on the experience that the conformation of small cyclic peptides is mainly determined by the chirality of the amino acids (and glycine or proline). For example, cyclic pentapeptides with one d and four l amino acids prefer a βII'/γ conformation. The sequence RGDFV was shifted around this spatial βII'/γ template by synthesis of five peptides in which one of the amino acids was used in d-configuration. It turned out that cyclo(-RGDfV-) is a selective inhibitor for the αvβ3 integrin, which is strongly expressed in cancer cells. Systematic variations with different turn mimetics, retro-inverso structures, modified peptide bonds and sugar amino acids are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00119142
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    Paper (German National Licenses)
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