Optimized Opioid-Neurotensin Multitarget Peptides: From Design to Structure-Activity Relationship Studies

J Med Chem. 2020 Nov 12;63(21):12929-12941. doi: 10.1021/acs.jmedchem.0c01376. Epub 2020 Sep 23.

Abstract

Fusion of nonopioid pharmacophores, such as neurotensin, with opioid ligands represents an attractive approach for pain treatment. Herein, the μ-/δ-opioid agonist tetrapeptide H-Dmt-d-Arg-Aba-β-Ala-NH2 (KGOP01) was fused to NT(8-13) analogues. Since the NTS1 receptor has been linked to adverse effects, selective MOR-NTS2 ligands are preferred. Modifications were introduced within the native NT sequence, particularly a β3-homo amino acid in position 8 and Tyr11 substitutions. Combination of β3hArg and Dmt led to peptide 7, a MOR agonist, showing the highest NTS2 affinity described to date (Ki = 3 pM) and good NTS1 affinity (Ki = 4 nM), providing a >1300-fold NTS2 selectivity. The (6-OH)Tic-containing analogue 9 also exhibited high NTS2 affinity (Ki = 1.7 nM), with low NTS1 affinity (Ki = 4.7 μM), resulting in an excellent NTS2 selectivity (>2700). In mice, hybrid 7 produced significant and prolonged antinociception (up to 8 h), as compared to the KGOP01 opioid parent compound.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Disease Models, Animal
  • Drug Design*
  • Humans
  • Male
  • Mice
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Oligopeptides / therapeutic use
  • Pain / drug therapy
  • Pain / pathology
  • Peptides / chemistry*
  • Peptides / metabolism
  • Peptides / therapeutic use
  • Protein Binding
  • Receptors, Neurotensin / chemistry
  • Receptors, Neurotensin / metabolism*
  • Receptors, Opioid, delta / agonists
  • Receptors, Opioid, delta / metabolism*
  • Receptors, Opioid, mu / agonists
  • Receptors, Opioid, mu / metabolism*
  • Structure-Activity Relationship

Substances

  • KGNOP1 peptide
  • Oligopeptides
  • Peptides
  • Receptors, Neurotensin
  • Receptors, Opioid, delta
  • Receptors, Opioid, mu