Nociceptin (1-13), amide is a potent ORL1 (OP4) receptor agonist with a pEC50 of 7.9 for mouse vas deferens and a Ki of 0.75 nM for binding to rat forebrain membranes.
CAT No: R1563
CAS No:178064-02-3
Synonyms/Alias:178064-02-3;N/OFQ-(1-13)-NH2;nociceptin(1-13)NH2;CHEMBL384755;Nociceptin (1-13), amide;Nociceptin (1-13) amide trifluoroacetate salt;OFQ/N;FGGFTGARKSARK;nociceptin (1-13) amide;orphanin FQ(1-13)NH2;Demethyl-AMPA;nociceptin/orphanin FQ(1-13)NH2;Nociceptin Orphanin FQ..1-13..-NH..2..;H-FGGFTGARKSARK-NH2;GTPL1682;BDBM85822;N/OFQ(1-13)NH2;NC(1-13)NH2;BDBM50106479;OFQ/N (1-11);AKOS024456547;NCGC00167157-01;DA-56231;FN109170;Q27087982;Phe-Gly-Gly-Phe-Thr-Gly-Ala-Arg-Lys-Ser-Ala-Arg-Lys-NH2;H-Phe-Gly-Gly-Phe-Thr-Gly-Ala-Arg-Lys-Ser-Ala-Arg-Lys-NH2; H-FGGFTGARKSARK-NH2;(2S)-6-amino-2-[(2S)-2-[(2S)-2-[(2S)-2-[(2S)-6-amino-2-[(2S)-2-[(2S)-2-{2-[(2S,3R)-2-[(2S)-2-(2-{2-[(2S)-2-amino-3-phenylpropanamido]acetamido}acetamido)-3-phenylpropanamido]-3-hydroxybutanamido]acetamido}propanamido]-5-carbamimidamidopentanamido]hexanamido]-3-hydroxypropanamido]propanamido]-5-carbamimidamidopentanamido]hexanamide;
Nociceptin (1-13), amide is a synthetic peptide fragment derived from the endogenous neuropeptide nociceptin, also known as orphanin FQ. Comprising the first thirteen amino acids of the full-length nociceptin sequence and featuring an amidated C-terminus, this peptide retains the biologically active core essential for receptor binding and downstream signaling. It is widely recognized for its role as a selective agonist of the nociceptin/orphanin FQ peptide (NOP) receptor, a member of the opioid receptor family, yet functionally distinct from classical opioid receptors. The unique structural and functional properties of this peptide make it an indispensable tool for researchers investigating the molecular mechanisms of nociceptin signaling, receptor pharmacology, and peptide-receptor interactions within the central nervous system and beyond.
Receptor pharmacology: Nociceptin (1-13), amide is extensively utilized in studies aiming to characterize the binding affinity, selectivity, and activation profile of the NOP receptor. Its well-defined structure allows for precise interrogation of receptor-ligand interactions, facilitating comparative analyses with other opioid receptor ligands. By using this peptide in binding assays and functional studies, researchers can elucidate the structural requirements for receptor activation and gain valuable insights into the pharmacological landscape of the NOP system.
Peptide structure-activity relationship (SAR) studies: The truncated and modified sequence of this peptide serves as a powerful model for dissecting the structural determinants of nociceptin activity. Investigators employ it to map critical residues responsible for biological activity, receptor affinity, and signaling efficacy. Such SAR studies contribute to the rational design of novel peptide analogs with tailored pharmacological profiles, supporting the development of selective NOP receptor modulators for basic research.
Neurobiological research: In neurochemical and physiological experiments, Nociceptin (1-13), amide is used to probe the functional roles of the NOP receptor in neuronal signaling pathways. Its application in electrophysiological recordings, neurotransmitter release assays, and synaptic plasticity models allows scientists to delineate the influence of NOP receptor activation on neuronal excitability, synaptic transmission, and network dynamics. These studies advance the understanding of nociceptin's involvement in central nervous system processes such as pain modulation, stress response, and behavioral regulation.
Peptide-receptor interaction modeling: The defined sequence and receptor specificity of this peptide make it a preferred reference ligand in computational modeling and biophysical studies. Researchers employ it in molecular docking simulations, NMR spectroscopy, and crystallography to visualize binding conformations and interaction networks within the NOP receptor binding pocket. These approaches provide a structural basis for interpreting experimental data and guiding the rational engineering of peptide-based ligands.
Analytical method development: Nociceptin (1-13), amide is also valued as a standard or control in the development and validation of analytical techniques for peptide detection and quantification. Its stability and well-characterized properties support the calibration of chromatographic or mass spectrometric assays, ensuring reliable measurement of peptide concentrations in complex biological matrices. This facilitates accurate monitoring of peptide pharmacokinetics and distribution in experimental systems, thereby enhancing the rigor of peptide research workflows.
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