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  • B1 kinin receptor  (2)
  • Binding  (1)
  • NK2  (1)
  • conformation  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Structural comparison of NK2 receptor agonists and antagonists (1994)
    Springer
    Journal of computer aided molecular design 8 (1994), S. 341-344 
    Details
    ISSN: 1573-4951
    Keywords: Tachykinins ; NK2 ; MEN-10627 ; Binding ; Agonist ; Antagonist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The conformational space of two NK2 receptor agonists and a new potent antagonist has been sampled by the simulated annealing technique. Low-energy conformers were obtained, which were compared with respect to their key residues, namely phenylalanine, leucine and methionine. The hypothesis is that they share part of the binding site on the receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00126750
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A structure-activity study on the bradykinin B1 antagonist desArg10-HOE 140: The alanine scan (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 123-127 
    Details
    ISSN: 1573-3904
    Keywords: B1 kinin receptor ; peptide antagonist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract It has recently been shown that the biological activity of the second generation kinin B1 receptor selective antagonist, desArg10 HOE 140, can be improved by specific amino acid substitutions. Starting from this observation, we undertook a systematic structure-activity relationship study of this antagonist, based on the alanine-scan technique, in order to obtain useful information for the rational design of more analogues. Our data indicate that the sequence of desArg10 HOE 140 does not tolerate the replacement by Ala of most of its residues, with the exception of Ser in position 7 and, to a lesser extent, D-Arg in position 1 and Hyp in position 4. The most critical residues appear to be Pro in position 3 and the C-terminal dipeptide DTic-Oic; Ala replacement at these positions resultes in a total loss of activity. Moreover, replacement by Ala of Gly in position 5 reverts the activity of desArg10 HOE 140 to that of an agonist.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008828104465
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  • 3
    Electronic Resource
    Electronic Resource
    A structure-activity study on the bradykinin B1 antagonist desArg10-HOE 140: The alanine scan (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 123-127 
    Details
    ISSN: 1573-3904
    Keywords: B1 kinin receptor ; peptide antagonist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary It has recently been shown that the biological activity of the second generation kinin B1 receptor selective antagonist, desArg10 HOE 140, can be improved by specific amino acid substitutions. Starting from this observation, we undertook a systematic structure-activity relationship study of this antagonist, based on the alanine-scan technique, in order to obtain useful information for the rational design of more analogues. Our data indicate that the sequence of desArg10 HOE 140 does not tolerate the replacement by Ala of most of its residues, with the exception of Ser in position 7 and, to a lesser extent, D-Arg in position 1 and Hyp in position 4. The most critical residues appear to be Pro in position 3 and the C-terminal dipeptide Dtic-Oic; Ala replacement at these positions resultes in a total loss of activity. Moreover, replacement by Ala of Gly in position 5 reverts the activity of desArg10 HOE 140 to that of an agonist.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443626
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  • 4
    Electronic Resource
    Electronic Resource
    Conformational rigidity versus flexibility in a novel peptidic neurokinin A receptor antagonist (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 236-240 
    Details
    ISSN: 1075-2617
    Keywords: Tachykinins ; NK-2 antagonist ; cyclic peptide ; conformation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Neurokinin A receptor antagonists have been proposed as a new class of drugs for several applications in humans (asthama, intestinal motility, etc.). The rational design, synthesis, structural characterization and biological activity evaluation of a new potent, highly selective, long-lasting, peptide-based receptor antagonist are reported. The structure-activity relationship indicates that the conformational rigidity determines potency, specificity and especially the long life of the molecule in the living body. MEN 10627 is the prototype of a new class of cyclic, peptide-based, neurokinin A receptor antagonists and it is a suitable candidate for clinical testing in humans.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010404
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