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  • 1
    Electronic Resource
    Electronic Resource
    Synthesis of RGD amphiphilic cyclic peptide as fibrinogen or fibronectin antagonist (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 455-461 
    Details
    ISSN: 1573-3904
    Keywords: Aggregometry ; Cyclic peptide ; Diazaethyleneglycol derivative ; HEL cell adhesion ; RGD peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary This paper investigates the effect of the incorporation of a diazaethylene glycol derivative (Deg,2) into a cyclic peptide containing the tripeptide sequence Arg-Gly-Asp (RGD). This motif is a common structural element of many integrin ligands. The synthesis of cyclo-(Arg-Gly-Asp-Deg) (7) has been accomplished in solution using standard peptide chemistry. The intent was to improve the bioavailability of this new RGD cyclic peptide, which is shown to interact with αIIbβ3 or α5β1 receptors. A preliminary step for the conformational study of peptide7 was done in DMSO-d 6 using nuclear magnetic resonance spectroscopy techniques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02442916
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of RGD amphiphilic cyclic peptide as fibrinogen or fibronectin antagonist (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 455-461 
    Details
    ISSN: 1573-3904
    Keywords: Aggregometry ; Cyclic peptide ; Diazaethyleneglycol derivative ; HEL cell adhesion ; RGD peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract This paper investigates the effect of the incorporation of adiazaethylene glycol derivative (Deg, 2) into a cyclic peptide containingthe tripeptide sequence Arg-Gly-Asp (RGD). This motif is a common structuralelement of many integrin ligands. The synthesis of cyclo-(Arg-Gly-Asp-Deg)(7) has been accomplished in solution using standard peptide chemistry. Theintent was to improve the bioavailability of this new RGD cyclic peptide,which is shown to interact with αIIbΒ3β3or α5 β1 receptors. A preliminary stepfor the conformational study of peptide 7 was done in DMSO-d6using nuclear magnetic resonance spectroscopy techniques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008844117525
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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