Design and synthesis of heterofunctional V(1a)-selective vasopressin receptor ligands with lysine at position 9

J. Howl, D. C. New, M. Wheatley

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

A peptide analogue of [8-arginine]vasopressin (AVP) with Lys substituted for Gly at position 9 ([d(CH2)5Tyr(Me)2LysNH29]AVP; ALVP) has been synthesized as a precursor for the production of heterofunctional vasopressin receptor ligands. Three heterofunctional ligands have been prepared by attaching biotin and a photoreactive cross-linker capable of iodination, either alone or in combination, to the ε-amino group of Lys at position 9 in ALVP. The binding characteristics of these novel ligands have been determined at the V(1a) and V2 vasopressin receptors by employing membrane preparations of rat liver and kidney respectively. All of the analogues synthesized during the course of this study bound selectively, and with high affinity, to the V(1a) vasopressin receptor subtype. Our results demonstrate that the strategies described in this paper provide a convenient means of synthesizing heterofunctional vasopressin receptor ligands with preservation of subtype-specific, high affinity binding characteristics. These parameters establish the potential value of the analogues as probes for investigating V(1a) receptor structure and function.

Original languageEnglish
Pages (from-to)123-129
Number of pages7
JournalJournal of Molecular Endocrinology
Volume9
Issue number2
DOIs
Publication statusPublished - 1992
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology

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