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  • B1 kinin receptor  (2)
  • Fmoc-Trp(Boc)-OH  (1)
  • Side reaction  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Solid support-dependent alkylation of tryptophan residues in SPPS using a 2-methoxybenzyl alcohol-based linker (1994)
    Springer
    International journal of peptide research and therapeutics 1 (1994), S. 149-155 
    Details
    ISSN: 1573-3904
    Keywords: Solid-phase peptide synthesis ; Side reaction ; Mass spectrometry ; Fmoc-Trp(Boc)-OH
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Several side reactions can be encountered in the synthesis of Trp-containing peptides, due to molecular species originating from side chain-protecting groups or from the linker during acidolytic cleavage of the peptide from the resin. The linker can be the source of both alkylation in solution of the indole moiety of the tryptophan side chain and permanent readdition of the cleaved peptide to the resin. We report that both these reactions occur at a high level during the synthesis of Trp-containing peptides on a PEG-PS resin containing a 2-methoxybenzyl alcohol-based linker, in spite of the presence of suitable scavengers in the TFA-based cleavage mixture. Both side reactions are efficiently prevented by the use of a protected analogue of tryptophan, namely Nim-Boc-Trp, previously reported for the synthesis of peptides containing tryptophan and arginine residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00128533
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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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    Paper (German National Licenses)
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