Noncompetitive nature of oxytocin antagonists with general structure Mpa(1)Xxx(2)Sar(7)Arg(8)

Peptides. 2002 Aug;23(8):1419-25. doi: 10.1016/s0196-9781(02)00082-7.

Abstract

Eight oxytocin (OT) antagonists with general structure Mpa(1)Sar(7)Arg(8), substituted at position 2 with conformationally constrained and bulky amino acids, were synthesized and pharmacologically tested. Binding affinities and selectivities of compounds for OT, and vasopressin receptor subtypes were investigated. In vitro effects of antagonists were evaluated via inhibition of OT-induced contractions of isolated guinea-pig uterus. The abilities of OT antagonists to inhibit spontaneous contractility in 24 h postpartum rat uterus were investigated. These peptides exhibited pseudoirreversible pharmacological properties, and comprise a novel group of OT antagonists for potential clinical use. Their noncompetitive pharmacological nature can be of therapeutic benefit through a sustained effect on myometrium.

MeSH terms

  • Animals
  • Female
  • Guinea Pigs
  • Hormone Antagonists / chemical synthesis
  • Hormone Antagonists / chemistry*
  • Hormone Antagonists / pharmacology*
  • Humans
  • Muscle Contraction / drug effects
  • Obstetric Labor, Premature / prevention & control
  • Oxytocin / antagonists & inhibitors*
  • Pregnancy
  • Protein Conformation
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, Oxytocin / metabolism*
  • Tocolytic Agents / chemical synthesis
  • Tocolytic Agents / chemistry*
  • Tocolytic Agents / pharmacology*
  • Uterus / metabolism

Substances

  • Hormone Antagonists
  • Receptors, Oxytocin
  • Tocolytic Agents
  • Oxytocin