Truncation of the peptide sequence in bifunctional ligands with mu and delta opioid receptor agonist and neurokinin 1 receptor antagonist activities

Bioorg Med Chem Lett. 2013 Sep 1;23(17):4975-8. doi: 10.1016/j.bmcl.2013.06.065. Epub 2013 Jul 2.

Abstract

The optimization and truncation of our lead peptide-derived ligand TY005 possessing eight amino-acid residues was performed. Among the synthesized derivatives, NP30 (Tyr(1)-DAla(2)-Gly(3)-Phe(4)-Gly(5)-Trp(6)-O-[3',5'-Bzl(CF3)2]) showed balanced and potent opioid agonist as well as substance P antagonist activities in isolated tissue-based assays, together with significant antinociceptive and antiallodynic activities in vivo.

Keywords: Bifunctional compounds; NMR structure; Neutokinin-1 receptor antagonists; Opioid receptor agonists; Truncation of peptide sequence.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Analgesics / chemistry
  • Analgesics / pharmacology
  • Analgesics / therapeutic use
  • Animals
  • Humans
  • Ligands
  • Neurokinin-1 Receptor Antagonists / chemistry*
  • Neurokinin-1 Receptor Antagonists / pharmacology*
  • Neurokinin-1 Receptor Antagonists / therapeutic use
  • Peptides / chemistry*
  • Peptides / pharmacology*
  • Peptides / therapeutic use
  • Rats
  • Receptors, Neurokinin-1 / metabolism
  • Receptors, Opioid, delta / agonists*
  • Receptors, Opioid, delta / metabolism
  • Receptors, Opioid, mu / agonists*
  • Receptors, Opioid, mu / metabolism

Substances

  • Analgesics
  • Ligands
  • Neurokinin-1 Receptor Antagonists
  • Peptides
  • Receptors, Neurokinin-1
  • Receptors, Opioid, delta
  • Receptors, Opioid, mu