Abstract：
:The peptide nociceptin/orphanin FQ (N/OFQ) and the N/OFQ receptor (NOP) constitute a neuropeptidergic system that modulates various biological functions and is currently targeted for the generation of innovative drugs. In the present study dimeric NOP receptor ligands with spacers of different lengths were generated using both peptide and non-peptide pharmacophores. The novel compounds (12 peptide and 7 nonpeptide ligands) were pharmacologically investigated in a calcium mobilization assay and in the mouse vas deferens bioassay. Both structure- and conformation-activity studies were performed. Results demonstrated that dimerization did not modify the pharmacological activity of both peptide and non-peptide pharmacophores. Moreover, when dimeric compounds were obtained with low potency peptide pharmacophores, dimerization recovered ligand potency. This effect depends on the doubling of the C-terminal address sequence rather than the presence of an additional N-terminal message sequence or modifications of peptide conformation.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Pacifico S,Carotenuto A,Brancaccio D,Novellino E,Marzola E,Ferrari F,Cerlesi MC,Trapella C,Preti D,Salvadori S,Calò G,Guerrini Rdoi
10.1038/srep45817subject
Has Abstractpub_date
2017-04-06 00:00:00pages
45817issn
2045-2322pii
srep45817journal_volume
7pub_type
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