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 opioid peptide derived from the prodynorphin precursor, recognized for its significant role in modulating pain perception and neurophysiological processes within the central nervous system. As a member of the endogenous opioid peptide family, Dynorphin (1-17) exhibits high affinity for kappa-opioid receptors, influencing a variety of cellular signaling pathways. Its unique amino acid sequence enables it to interact with specific receptor subtypes, facilitating intricate regulatory functions that have made it an essential tool in neuroscience research. The peptide's capacity to mimic endogenous neuropeptide activity provides researchers with a valuable means to investigate complex neural networks and neurotransmitter systems, advancing our understanding of brain function and pathophysiology.
Neuroscience Research: Dynorphin (1-17) serves as a critical probe in neuroscience studies aimed at elucidating the mechanisms of pain modulation, stress response, and emotional regulation. By selectively activating kappa-opioid receptors, this peptide allows researchers to dissect the roles of endogenous opioids in synaptic transmission, neuronal excitability, and neuroplasticity. Its application in in vitro and in vivo models enables the mapping of dynorphinergic pathways, contributing to the identification of novel targets for neuropsychiatric and neurodegenerative disorder investigations. The ability to modulate receptor activity with high specificity makes it an indispensable reagent for exploring the physiological and pathological functions of the opioid system.
Addiction and Substance Abuse Studies: In the context of addiction research, Dynorphin (1-17) is frequently utilized to investigate the neurochemical adaptations associated with chronic exposure to drugs of abuse. Through its interaction with kappa-opioid receptors, the peptide is instrumental in modeling the negative affective states and dysphoric responses that often accompany withdrawal and relapse. By examining how dynorphin signaling influences dopamine release and reward circuitry, researchers gain insights into the molecular underpinnings of substance dependence. These studies inform the development of targeted interventions aimed at mitigating the adverse effects of addiction and promoting recovery.
Pain Pathway Analysis: Dynorphin (1-17) is widely employed in the study of pain transmission and modulation, particularly in preclinical models of acute and chronic pain. By simulating endogenous peptide release, it allows for the detailed examination of spinal and supraspinal mechanisms that govern nociceptive processing. Researchers utilize this peptide to assess the contribution of kappa-opioid receptor activation to analgesic and hyperalgesic responses, offering a deeper understanding of the dynamic interplay between excitatory and inhibitory signaling in pain pathways. Such investigations support the identification of novel molecular targets for pain management strategies.
Mood and Stress Regulation: The use of Dynorphin (1-17) extends to research on mood disorders and stress-related conditions. Its modulatory effects on neurotransmitter systems, including dopamine and glutamate, provide a foundation for exploring the biochemical basis of anxiety, depression, and stress resilience. Experimental models employing this peptide help delineate the role of endogenous opioid peptides in emotional behavior and adaptive responses to environmental stressors. These findings contribute to a broader comprehension of the neurobiological substrates underlying affective disorders.
Cell Signaling and Molecular Pharmacology: Dynorphin (1-17) is a valuable tool in molecular pharmacology for characterizing G protein-coupled receptor (GPCR) signaling pathways. By binding to and activating kappa-opioid receptors, the peptide enables the study of downstream signaling cascades such as inhibition of adenylate cyclase, modulation of ion channel activity, and regulation of intracellular second messengers. These mechanistic insights are fundamental for understanding receptor pharmacodynamics and for the rational design of novel ligands with therapeutic potential. The peptide's versatility in experimental assays underscores its importance in advancing receptor biology and drug discovery efforts.
Behavioral Neuroscience Investigations: Researchers utilize Dynorphin (1-17) in behavioral paradigms to assess its impact on locomotor activity, learning, memory, and social interaction. By modulating endogenous opioid tone, it provides a means to investigate the relationship between neuropeptide signaling and complex behavioral phenotypes. These studies shed light on the functional relevance of dynorphinergic systems in regulating cognitive and affective processes, paving the way for new approaches in the study of neurobehavioral disorders.
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.
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