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) is a synthetic peptide corresponding to the first thirteen amino acids of the endogenous opioid peptide dynorphin A. As a naturally occurring neuropeptide, it plays a central role in the modulation of pain, stress response, and various neurophysiological processes through its high-affinity interaction with kappa-opioid receptors in the central nervous system. Its unique sequence and functional properties make it a valuable tool for probing the molecular mechanisms of opioid signaling, receptor selectivity, and peptide-receptor interactions. Due to its relevance in neurobiology and pharmacology, Dynorphin A(1-13) is widely utilized in both fundamental and applied research settings where precise modulation of opioid pathways is required.
Receptor binding studies: Dynorphin A(1-13) is extensively used to investigate the binding characteristics and functional responses of kappa-opioid receptors. Its well-defined structure allows researchers to characterize receptor-ligand interactions, assess binding affinity, and elucidate receptor subtypes' pharmacological profiles. By employing this peptide in radioligand binding assays or functional bioassays, scientists can gain insights into opioid receptor activation, desensitization, and downstream signaling cascades, thus advancing the understanding of opioid pharmacodynamics.
Neuropharmacology research: In neuropharmacological studies, Dynorphin A(1-13) serves as a selective agonist to model endogenous opioid activity. Researchers utilize it to dissect the role of kappa-opioid receptor pathways in modulating nociception, stress adaptation, and emotional regulation. Its application in in vitro neuronal cultures or in vivo animal models facilitates the exploration of synaptic transmission, neurotransmitter release, and the broader implications of opioid system dysregulation in neurological disorders.
Peptide structure-activity relationship analysis: The defined sequence of Dynorphin A(1-13) provides an excellent template for structure-activity relationship (SAR) studies. By introducing systematic modifications or truncations to the peptide, scientists can map critical residues responsible for receptor affinity, selectivity, and efficacy. Such SAR investigations inform the rational design of novel peptide analogs with tailored pharmacological properties, supporting the development of next-generation research tools and potential therapeutic leads.
Peptide synthesis and analytical method development: As a standard reference peptide, Dynorphin A(1-13) is frequently employed in the optimization and validation of solid-phase peptide synthesis protocols and analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its use as a benchmark compound aids in assessing peptide purity, sequence fidelity, and analytical method sensitivity, thereby supporting quality control and reproducibility in peptide chemistry workflows.
Cell signaling pathway elucidation: By serving as a potent kappa-opioid receptor agonist, Dynorphin A(1-13) enables researchers to dissect intracellular signaling mechanisms triggered by receptor activation. Application of the peptide in cellular assays allows for the monitoring of G-protein coupling, second messenger generation, and downstream effector modulation. These studies contribute to a deeper understanding of how opioid peptides influence complex signaling networks, providing a foundation for further exploration of neurochemical pathways relevant to pain, mood regulation, and stress physiology.
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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