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Updated: May 20, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Study of the N-terminal part of peptidic selective NPFF₂ agonists
Honoré Mazarguil1, Catherine Mollereau, Georges Czaplicki
1Institut de Pharmacologie et de Biologie Structurale, CNRS/Université de Toulouse UMR 5089, 205 Route de Narbonne, 31077 Toulouse Cedex, France.
Abstract:
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.
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