Synthesis and biological activity of LH-RH antagonists modified in position 1

Aniko Horvath, David H. Coy, Mary V. Nekola, Esther J. Coy, Andrew V. Schally, Istvan Teplan

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28 Scopus citations

Abstract

As part of our studies on the design of more potent antagonists of the LH-RH (luteinizing hormone-releasing hormone) decapeptide, twelve new highly soluble D-Arg6-analogs have been synthesized. These peptides contain modifications in position 1 and are typified by the general formula (N-acetyl-X1, D-p-Cl-Phe2, D-Trp3, D-Arg6, D-Ala10) LH-RH. We have found that a lypophilic, aromatic substituent is required in position 1 in order to elicit antiovulatory activity at a dose as low as 3 μg. The larger the hydrophobic amino acid (X: p-Br-Phe, β-Nal-2) in position 1, the higher is the antiovulatory activity that can be attained. Analogs with non-aromatic or hydrophilic amino acids (X: Gly, Leu, Arg, His, Glu) in position 1 generally have much lower activities in this series of LH-RH antagonists.

Original languageEnglish (US)
Pages (from-to)969-971
Number of pages3
JournalPeptides
Volume3
Issue number6
DOIs
StatePublished - Jan 1 1982
Externally publishedYes

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Keywords

  • Antiovulatory activity
  • LH-RH antagonists
  • Peptide synthesis

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

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