Study of the N-terminal part of peptidic selective NPFF₂ agonists.

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.

journal_name

Peptides

journal_title

Peptides

authors

Mazarguil H,Mollereau C,Czaplicki G,Zajac JM

doi

10.1016/j.peptides.2012.07.008

subject

Has Abstract

pub_date

2012-09-01 00:00:00

pages

157-60

issue

1

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(12)00307-5

journal_volume

37

pub_type

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