Dynorphin B (1-13) acts as an agonist on opioid κ-receptor.
CAT No: R1332
CAS No:83335-41-5
Synonyms/Alias:Rimorphin;Dynorphin B;83335-41-5;Dynorphin B porcine;Dynorphin B (swine);K41YC3AEI8;RIMORPHIN (OX);DYNORPHIN B (OX);DYNORPHIN B (PIG);DYNORPHIN B (RAT);UNII-K41YC3AEI8;DYNORPHIN B (HUMAN);Dynorphin B (1-13);Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr;85006-82-2;L-THREONINE, L-TYROSYLGLYCYLGLYCYL-L-PHENYLALANYL-L-LEUCYL-L-ARGINYL-L-ARGINYL-L-GLUTAMINYL-L-PHENYLALANYL-L-LYSYL-L-VALYL-L-VALYL-;Dynorphin B trifluoroacetate salt;DYNORPHIN B-OH;CHEMBL500830;GTPL1622;BDBM85325;AKOS024457470;Dynorphin B porcine, >=95% (HPLC);NCGC00163206-01;NCGC00163206-02;DA-63065;FD108736;H-Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr-OH; H-YGGFLRRQFKVVT-OH;
Dynorphin B 1-13 is a synthetic peptide fragment derived from the endogenous opioid peptide dynorphin B, part of the prodynorphin gene family. As a member of the opioid peptide group, it is characterized by its affinity for kappa-opioid receptors and its involvement in modulating nociceptive pathways in the central nervous system. The unique sequence and structure of Dynorphin B 1-13 confer distinct receptor selectivity and biological activity, making it a valuable tool for exploring the roles of endogenous opioids in neurobiology. Its biochemical properties are of particular relevance in studies focused on pain modulation, neurotransmission, and the physiological functions of opioid peptides.
Receptor Pharmacology: Dynorphin B 1-13 is widely utilized in receptor binding studies to characterize the pharmacological properties of kappa-opioid receptors. Researchers employ this peptide to assess ligand-receptor interactions, determine binding affinities, and elucidate receptor subtypes across various tissues. The ability of Dynorphin B 1-13 to selectively engage kappa-opioid receptors enables detailed investigations into receptor signaling pathways, ligand specificity, and the molecular determinants of opioid receptor activation.
Neurobiological Research: In neuroscience, Dynorphin B 1-13 serves as a critical probe for dissecting the functional roles of endogenous opioid peptides in the central nervous system. Experimental models frequently use this peptide to investigate mechanisms underlying pain perception, stress response, and neuroendocrine regulation. By modulating synaptic transmission and neuronal excitability, it facilitates the study of complex neurophysiological processes and contributes to a deeper understanding of opioid-mediated signaling networks.
Peptide Structure-Activity Relationship Studies: The defined amino acid sequence of Dynorphin B 1-13 makes it an ideal candidate for structure-activity relationship (SAR) analyses. Researchers can systematically modify its sequence to evaluate the impact of specific residues on receptor binding, biological activity, and metabolic stability. These SAR investigations provide valuable insights into the molecular features governing peptide-receptor interactions and inform the rational design of novel peptide analogs with tailored pharmacological profiles.
Peptide-Based Assay Development: Dynorphin B 1-13 is frequently employed as a reference standard or functional ligand in the development and validation of biochemical assays targeting opioid receptors. Its well-characterized activity profile supports the calibration of receptor binding assays, functional response measurements, and high-throughput screening platforms. These applications are essential for assessing the efficacy and selectivity of new opioid ligands in a controlled experimental context.
Biochemical Mechanism Elucidation: The peptide is instrumental in mechanistic studies aimed at deciphering the intracellular signaling cascades triggered by kappa-opioid receptor activation. By applying Dynorphin B 1-13 in in vitro and ex vivo systems, researchers can monitor downstream events such as G-protein coupling, second messenger production, and ion channel modulation. Such investigations enhance the overall understanding of opioid receptor signaling dynamics and their broader physiological implications.
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