Tryptophan replacement in the nociceptin/orphanin FQ receptor ligand Ac-RYYRWK-NH2.

G Carra', G Calo', B Spagnolo, R Guerrini, M Arduin, E Marzola, C Trapella, D Regoli, S Salvadori
Author Information
  1. G Carra': Section of Pharmacology and Neuroscience Centre, Department of Experimental and Clinical Medicine, University of Ferrara, 44100 Ferrara, Italy.

Abstract

In the present study we describe the in vitro pharmacological characterization of the nociceptin/orphanin FQ (N/OFQ) receptor (NOP) ligand Ac-RYYRWK-NH2 and the synthesis and biological evaluation of 13 Trp5 substituted Ac-RYYRWK-NH2 analogs. Results indicate that Ac-RYYRWK-NH2 behaves as a highly potent and selective partial agonist at the NOP receptors and that the whole indole moiety of the Trp5 side chain is not required, being a phenyl-ethyl side chain already sufficient for maintaining high potency.

Grants

  1. R01HL71212/NHLBI NIH HHS

MeSH Term

Amino Acid Sequence
Amino Acids, Aromatic
Animals
Cells, Cultured
Dose-Response Relationship, Drug
Electric Stimulation
Male
Mice
Mice, Knockout
Oligopeptides
Opioid Peptides
Structure-Activity Relationship
Tryptophan
Vas Deferens
Nociceptin

Chemicals

(Nphe(1),Arg(14),Lys(15))N-OFQ NH(2)
Amino Acids, Aromatic
CAM 6369
Oligopeptides
Opioid Peptides
Tryptophan