Study of the N-terminal part of peptidic selective NPFF₂ agonists.
Neuropeptide FF (NPFF) has been shown to act as an endogenous anti-analgesic peptide. In this paper, several peptide analogs of the selective ligand dNP(NMe)AFLFQPQRF-NH(2) modified in the putative address segment, were designed to be selective NPFF(2) receptor probes, synthesized and assayed. One peptide dA(NMe)AAFLFQPQRF-NH(2) displays a very high affinity for NPFF(2) receptors transfected in CHO cells, and a high selectivity versus NPFF(1) receptors. The exact residues carried in the N-terminal part of the ligands are not decisive to obtain a high affinity only the length of the peptide in itself seems important to create selectivity.
Institut de Pharmacologie et de Biologie Structurale, CNRS/Université de Toulouse UMR 5089, 205 Route de Narbonne, 31077 Toulouse Cedex, France.
Honoré
H
Mazarguil
Catherine
C
Mollereau
Georges
G
Czaplicki
Jean-Marie
JM
Zajac
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D006801:Humans; D008024:Ligands; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D018013:Receptors, Neuropeptide / Q000819:agonists* / Q000378:metabolism
D008024:Ligands; D010446:Peptide Fragments; D018013:Receptors, Neuropeptide; C083929:neuropeptide FF receptor