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
Peptidesjournal_title
Peptidesauthors
Mazarguil H,Mollereau C,Czaplicki G,Zajac JMdoi
10.1016/j.peptides.2012.07.008subject
Has Abstractpub_date
2012-09-01 00:00:00pages
157-60issue
1eissn
0196-9781issn
1873-5169pii
S0196-9781(12)00307-5journal_volume
37pub_type
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