Dynorphin A-( 1- 17) is an endogenous opioid derived from the prohormone prodynorphin. It acts as endogenous κ-agonist that is resistant to enzymatic degradation. And it is a neuroactive peptide with potent analgesic effects.
CAT No: 10-101-81
CAS No:80448-90-4
Synonyms/Alias:Dynorphin A (swine);80448-90-4;Dynorphin A (1-17);Dynorphin A1-17;Dynorphin A trifluoroacetate salt;9M18T0TD14;Dynorphin (1-17);UNII-9M18T0TD14;Dynorphin A porcine;Dynorphin-(1-17);DYNORPHIN A (HUMAN);Dynorphin A amide, porcine;Dynorphin 17;DYNORPHIN [MI];DYNORPHIN A (PIG);DYNORPHIN A (RAT);DYN-A17;Dyn A 1-17;DYNORPHIN A (PORCINE);DYNORPHIN A (BOS TAURUS);JMNJYGMAUMANNW-FIXZTSJVSA-N;BDBM50096785;MFCD00076351;MFCD00079857;AKOS024457469;PORCINE DYNORPHIN A (1-17);Dynorphin A porcine, >=95% (HPLC);NCGC00167144-01;DA-72948;FD108724;F87314;H-Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln-OH; H-YGGFLRRIRPKLKWDNQ-OH;
Chemical Name:(2S)-5-amino-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-1-[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylpentanoyl]amino]-5-carbamimidamidopentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-carboxypropanoyl]amino]-4-oxobutanoyl]amino]-5-oxopentanoic acid
Dynorphin (1-17) is a naturally occurring endogenous opioid peptide composed of 17 amino acids, derived from the prodynorphin precursor protein. As a member of the dynorphin family, it plays a critical role in modulating pain perception, stress response, and neurochemical signaling within the central nervous system. Its high affinity for kappa-opioid receptors distinguishes it from other opioid peptides, making it a valuable tool for researchers investigating the molecular mechanisms underlying opioid receptor function, neuropeptide signaling, and the physiological pathways influenced by endogenous opioids. The unique sequence and receptor selectivity of Dynorphin (1-17) have established its significance in neuropharmacological studies and peptide research.
Opioid Receptor Research: Dynorphin (1-17) is extensively utilized in the study of opioid receptor pharmacology, particularly for elucidating the structure, function, and signaling pathways of kappa-opioid receptors (KORs). Its selective binding enables researchers to dissect receptor-ligand interactions, assess receptor activation or desensitization, and explore the downstream effects of kappa-opioid receptor engagement. Insights gained from these studies contribute to a deeper understanding of endogenous opioid systems and support the development of novel receptor-targeted probes or modulators for research purposes.
Neuropeptide Signaling Pathways: As a prototypical endogenous opioid peptide, Dynorphin (1-17) serves as a model system for investigating neuropeptide-mediated signaling in neuronal and glial cells. Researchers employ this peptide to examine the dynamics of neuropeptide release, receptor-mediated signal transduction, and cross-talk with other neurotransmitter systems. Its application in in vitro and ex vivo models aids in mapping the distribution of opioid peptides, characterizing receptor subtype specificity, and elucidating the regulatory mechanisms that govern neuropeptide function in the brain and spinal cord.
Pain Mechanism Studies: The role of Dynorphin (1-17) in modulating nociceptive transmission and pain processing is a central focus in neurobiology and pain research. Experimental models utilizing this peptide allow for the investigation of endogenous pain control circuits, the identification of molecular targets involved in hyperalgesia or analgesia, and the exploration of adaptive changes following chronic pain or injury. By providing a controlled means to activate kappa-opioid pathways, Dynorphin (1-17) enables researchers to differentiate between the physiological and pathophysiological roles of opioid peptides in pain modulation.
Peptide Structure-Activity Relationship Analysis: The defined sequence and receptor selectivity of Dynorphin (1-17) make it an important reference compound in structure-activity relationship (SAR) studies of opioid peptides. Through systematic modification or truncation of its amino acid sequence, researchers can probe the structural determinants responsible for receptor affinity, efficacy, and selectivity. SAR investigations using this peptide inform the rational design of new analogs, functional probes, or peptide-based tools for dissecting opioid receptor pharmacology and neuropeptide signaling.
Analytical Method Development: Dynorphin (1-17) is frequently employed as a standard or reference material in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its well-characterized physicochemical properties and biological activity support the calibration of detection methods, quantification of endogenous opioid peptides in biological samples, and assessment of assay specificity and sensitivity. These analytical applications are essential for advancing neurochemical research and ensuring the reliability of experimental data involving neuropeptides.
Dynorphin 1–17, (DYN 1–17) opioid peptide produces antinociception following binding to the kappa-opioid peptide (KOP) receptor. Upon synthesis and release in inflamed tissues by immune cells, DYN 1–17 undergoes rapid biotransformation and yields a unique set of opioid and non-opioid fragments. Some of these major fragments possess a role in immunomodulation, suggesting that opioid-targeted therapeutics may be effective in diminishing the severity of inflammatory disorders.
Rahiman, S. S. F., Morgan, M., Gray, P., Shaw, P. N., & Cabot, P. J. (2016). Dynorphin 1-17 and Its N-Terminal Biotransformation Fragments Modulate Lipopolysaccharide-Stimulated Nuclear Factor-kappa B Nuclear Translocation, Interleukin-1beta and Tumor Necrosis Factor-alpha in Differentiated THP-1 Cells. PloS one, 11(4), e0153005.
Dynorphin A (1–17), an endogenous opioid neuropeptide, can have pathophysiological consequences at high concentrations through actions involving glutamate receptors. Despite evidence of excitotoxicity, the basic mechanisms underlying dynorphin-induced cell death have not been explored. To address this question, we examined the role of caspase-dependent apoptotic events in mediating dynorphin A (1–17) toxicity in embryonic mouse striatal neuron cultures. In addition, the role of opioid and/or glutamate receptors were assessed pharmacologically using MK(+)801, a non-equilibrium N-methyl-D-aspartate (NMDA) antagonist; CNQX, a competitive α-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA)/kainate antagonist; or (−)-naloxone, a general opioid antagonist.
Singh, I. N., Goody, R. J., Goebel, S. M., Martin, K. M., Knapp, P. E., Marinova, Z., ... & Hauser, K. F. (2003). Dynorphin A (1–17) induces apoptosis in striatal neurons in vitro through α-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate receptor-mediated cytochrome C release and caspase-3 activation. Neuroscience, 122(4), 1013-1023.
Opioids inhibit release of primary afferent transmitters but it is unclear whether the converse occurs. To test the hypothesis that primary afferent transmitters influence opioid-ergic tone, we studied the functional and anatomical relationships between pituitary adenylyl cyclase-activating polypeptide (PACAP) and dynorphin 1-17 (Dyn) in spinal cord. We found that activation of the PACAP-specific receptor PAC1 (PAC1R) inhibited, whereas PAC1R blockade augmented, spinal release of Dyn. It is noteworthy that in the formalin-induced pain model PAC1R blockade (via PACAP6-38) also resulted in antinociception that was abolished by spinal κ-opioid receptor blockade.
Liu, N. J., Schnell, S. A., Schulz, S., Wessendorf, M. W., & Gintzler, A. R. (2011). Regulation of spinal dynorphin 1-17 release by endogenous pituitary adenylyl cyclase-activating polypeptide in the male rat: relevance of excitation via disinhibition. Journal of Pharmacology and Experimental Therapeutics, 336(2), 328-335.
1. TMEM16F and dynamins control expansive plasma membrane reservoirs
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4. High fat diet and GLP-1 drugs induce pancreatic injury in mice
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