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  • Articles  (2)
  • Inhibition  (1)
  • MALDI-TOF-MS  (1)
  • Springer  (2)
  • American Meteorological Society (AMS)
  • Berlin: Deutsches Institut für Wirtschaftsforschung (DIW)
  • 1995-1999  (2)
  • 1925-1929
  • Chemistry and Pharmacology  (2)
Collection
  • Articles  (2)
Source
Keywords
Publisher
  • Springer  (2)
  • American Meteorological Society (AMS)
  • Berlin: Deutsches Institut für Wirtschaftsforschung (DIW)
Years
  • 1995-1999  (2)
  • 1925-1929
Year
Topic
  • Chemistry and Pharmacology  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Host-cell-specific glycosylation of HIV-2 envelope glycoprotein (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 785-793 
    Details
    ISSN: 1573-4986
    Keywords: glycoprotein ; glycosylation ; gp120 ; HIV ; MALDI-TOF-MS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Neutral complex-type N-glycans of the envelope glycoprotein 120 of HIV-2, propagated in different host cells, display cell-type specific variations. In order to identify typical structural elements, glycans were analysed by gel filtration, by enzymic sequencing and, in part, by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The characteristic substituents of di- tri- and tetraantennary carbohydrate units thus observed include N-acetyllactosamine repeats, bisecting N-acetylglucosamine and fucose linked to the chitobiose core as well as to N-acetyllactosamine antennae. Each glycoprotein preparation displayed a characteristic set of glycoforms. Abbreviations: endo H, endo-β-N-acetylglucosaminidase H; E-PHA, Phaseolus vulgaris agglutinin E4; GlcNAcOH, N-acetyl-glucosaminitol; gp120/HUT78(MOLT4/Mφ/PBL/U937), external envelope glycoprotein 120 of HIV-2, strain D194, propagated in HUT78 (MOLT4, Mφ, PBL, U937) cells; gu, glucose units; HPAEC, high-pH anion-exchange chromatography; MALDI-TOF-MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; Mφ, human monocytes/macrophages; PBL, human peripheral blood lymphocytes; PNGase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018577619036
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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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