Dynorphin A(1-13), a version of dynorphin A containing only the first 13 amino acids of the peptide, in the rat spinal cord has additive effects.
CAT No: 10-101-12
CAS No:72957-38-1 (net)
Synonyms/Alias:dynorphin (1-13); dinorphinA (1-13); Dynorphin A; DynorphinA; Dynorphin-A; Dynorphin 1-13; Dynorphin1-13; dynorphin(1-13); 1-13-Dynorphin A; LS-63662; LS63662; LS 63662;L-tyrosyl-glycyl-glycyl-L-phenylalanyl-L-leucyl-L-arginyl-L-arginyl-L-isoleucyl-L-arginyl-L-prolyl-L-lysyl-L-leucyl-L-lysine
Chemical Name:(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-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-methylpentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]hexanoic acid
Dynorphin A(1-13), a naturally occurring endogenous opioid peptide, is a significant research tool in neurobiology and molecular pharmacology. As a member of the dynorphin family, this peptide consists of the first thirteen amino acids of the full-length dynorphin A sequence, conferring it with unique receptor-binding properties and biological activities. Its high affinity for kappa opioid receptors makes it invaluable for probing the complexities of opioid signaling pathways in the central nervous system. Researchers appreciate the structural stability and bioactivity of Dynorphin A(1-13), which facilitate investigations into neuromodulation, pain perception, and the physiological roles of endogenous opioids. The peptide's utility extends to studies of synaptic transmission, receptor selectivity, and the molecular basis of addiction and stress responses, making it a versatile compound for a variety of experimental frameworks.
Neuroscience research: Dynorphin A(1-13) serves as a fundamental tool for elucidating the mechanisms underlying opioid receptor signaling in the brain and spinal cord. By selectively activating kappa opioid receptors, this peptide enables scientists to dissect the roles of endogenous opioids in modulating synaptic activity, neurotransmitter release, and neuronal excitability. Its application in electrophysiological assays and in vitro models has advanced our understanding of how dynorphins influence neural circuitry involved in pain, mood regulation, and reward processing. The peptide's unique receptor selectivity also facilitates the investigation of receptor cross-talk and signaling cascades, providing deeper insights into the molecular determinants of opioid-mediated effects.
Pain mechanism studies: As a potent kappa opioid receptor agonist, Dynorphin A(1-13) is widely utilized in experimental models to investigate the molecular and cellular underpinnings of nociception and pain modulation. Researchers employ this peptide to induce or inhibit pain responses, allowing for the dissection of spinal and supraspinal pathways involved in analgesia and hyperalgesia. By modulating neurotransmitter systems and interacting with specific receptor subtypes, Dynorphin A(1-13) helps clarify the contribution of endogenous opioids to both acute and chronic pain states. These studies are instrumental in identifying novel therapeutic targets for pain management and in understanding the complex interplay between different opioid peptides within the nervous system.
Addiction and substance abuse research: The role of Dynorphin A(1-13) in the regulation of reward pathways has made it a key molecule for addiction biology studies. Its action on kappa opioid receptors has been shown to modulate dopamine release and influence behavioral responses to drugs of abuse. By administering the peptide in various animal models, researchers can explore how alterations in dynorphin signaling affect drug-seeking behavior, withdrawal symptoms, and relapse. These insights are critical for unraveling the neurochemical basis of addiction and for identifying potential strategies to mitigate substance abuse disorders through modulation of endogenous opioid systems.
Stress and emotional regulation: Dynorphin A(1-13) is instrumental in research exploring the neurobiological mechanisms of stress and emotional processing. Its interaction with kappa opioid receptors has been implicated in the modulation of stress-induced behaviors, anxiety, and mood disorders. Studies utilizing this peptide have demonstrated its ability to alter hypothalamic-pituitary-adrenal axis activity and influence neuroendocrine responses to stressors. By examining the effects of Dynorphin A(1-13) on emotional regulation, scientists gain valuable information on the links between opioid signaling, affective states, and vulnerability to psychiatric conditions.
Neurodegenerative disease models: Dynorphin A(1-13) also finds application in the study of neurodegenerative disorders, where disruptions in opioid signaling are believed to contribute to disease progression and symptomatology. The peptide is used to investigate its impact on neuronal survival, synaptic plasticity, and neuroinflammatory processes in models of diseases such as Alzheimer's and Parkinson's. By modulating kappa opioid receptor activity, Dynorphin A(1-13) allows researchers to probe the potential neuroprotective or neurotoxic effects of endogenous opioids, thereby advancing our understanding of disease mechanisms and the search for novel neurotherapeutic approaches. Through these diverse research applications, Dynorphin A(1-13) continues to be an essential compound for advancing neuropharmacological and neurobiological science.
Dynorphin A is an endogenous opioid peptide that preferentially activates κ opioid receptors and is antinociceptive at physiological concentrations. Levels of dynorphin A and a major metabolite, dynorphin A (1-13), increase significantly following spinal cord trauma and reportedly contribute to neurodegeneration associated with secondary injury. Interestingly, both κ opioid and N-methyl-D-aspartate (NMDA) receptor antagonists can modulate dynorphin toxicity, suggesting that dynorphin is acting (directly or indirectly) through κ opioid and/or NMDA receptor (NMDAR) types. Despite these findings, few studies have systematically explored dynorphin toxicity at the cellular level in defined populations of neurons co-expressing κ opioid and NMDA receptors.
Hauser, K. F., Foldes, J. K., & Turbek, C. S. (1999). Dynorphin A (1–13) neurotoxicity in vitro: opioid and non-opioid mechanisms in mouse spinal cord neurons. Experimental neurology, 160(2), 361-375.
We describe the opioid properties of a tridecapeptide, the sequence of which corresponds to the NH2-terminal sequence of dynorphin, a novel porcine pituitary endorphin. It contains [Leu]enkephalin. In the guinea pig ileum longitudinal muscle preparation it is about 700 times more potent than [Leu]enkephalin. Its effects in this tissue are blocked completely by naloxone, but the apparent affinity of naloxone is 1/13th that for blockade of [Leu]enkephalin or normorphine. In the mouse vas deferens, this peptide is 3 times more potent than [Leu]enkephalin. Well-washed rat brain membranes degrade the peptide rapidly, suggesting the presence of a membrane-bound degradative enzyme. The peptide displays considerable immunoreactivity in assays with antisera that have been used for the immunohistochemical localization of [Leu]enkephalin. The remarkable enhancement of the potency of [Leu]enkephalin by the COOH-terminal extension -Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-OH suggests new interpretations concerning the structure of opiate receptors and the function of the enkephalin pentapeptides.
Goldstein, A., Tachibana, S., Lowney, L. I., Hunkapiller, M., & Hood, L. (1979). Dynorphin-(1-13), an extraordinarily potent opioid peptide. Proceedings of the National Academy of Sciences, 76(12), 6666-6670.
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