Pharmacology letter accelerated communicationOrphanin FQ: Receptor binding and analog structure activity relationships in rat brain
References (15)
- et al.
FEBS Letters
(1994) - et al.
FEBS Lett.
(1994) - et al.
FEBS Lett.
(1994) - et al.
FEBS Lett.
(1994) - et al.
Mol. Brain Res.
(1994) - et al.
FEBS Lett.
(1994) Anal. Biochem.
(1976)
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Biochemical and pharmacological investigation of novel nociceptin/OFQ analogues and N/OFQ-RYYRIK hybrid peptides
2019, PeptidesCitation Excerpt :Molecular dynamics simulations suggest that N/OFQ (14–17) does not interact with the NOP receptor [15]. This may be explained by the SAR studies, which show that the shortest active fragment of nociceptin is N/OFQ (1–13) [16,17]. It has been reported that Dooley's hexapeptides such as Ac-RYYRIK-NH2 competitively inhibited N/OFQ binding to the NOP receptor [18] and therefore their binding sites may overlap [19].
Peptide welding technology – A simple strategy for generating innovative ligands for G protein coupled receptors
2018, PeptidesCitation Excerpt :This result contrasts with previous findings demonstrating long lasting actions of PWT derivatives which has been interpreted as due to lower susceptibility to peptidases [25]. Previous studies demonstrated that aminopeptidase recognizes N/OFQ as a substrate [62] generating [desPhe1]N/OFQ a peptide lacking affinity for the NOP receptor [63]. Eventually the presence of the unnatural amino acid Nphe at position 1 of UFP-101 may confer to this compound some resistance to peptidases that is not further increased by the PWT chemical modification.
Structure activity studies of nociceptin/orphanin FQ(1-13)-NH<inf>2</inf> derivatives modified in position 5
2015, Bioorganic and Medicinal ChemistryCitation Excerpt :Similar results were obtained using the smallest chiral residue Ala (compound 11). This confirms previous data obtained in classical Ala-scan studies.4,21 The increase in peptide flexibility obtained using the non chiral residue Gly produced a moderate loss of potency.
Helix-Constrained Nociceptin Peptides Are Potent Agonists and Antagonists of ORL-1 and Nociception
2015, Vitamins and HormonesCitation Excerpt :The address domain of nociceptin (i.e., residues 7–17) contains basic amino acid residues that likely bind to acidic residues present in the second extracellular loop of the ORL-1 receptor (Thompson et al., 2012). Nociceptin (nociceptin(1–17)-OH) is equipotent with its amidated form (nociceptin(1–17)-NH2; Guerrini et al., 1997), yet truncation of the nociceptin sequence possessing either a free acid or an amidated C-terminus resulted in substantial changes in binding affinity for ORL-1 (Butour et al., 1997; Calo et al., 1997; Dooley & Houghten, 1996; Guerrini et al., 1997). C-terminal truncation of nociceptin-(1–17)-OH, for instance, induced lower binding affinity and biological potency at the ORL-1 receptor (Butour et al., 1997; Reinscheid et al., 1996).