Adrenorphin is widely distributed throughout the mammalian brain. It has strong opioid activity, can be used as an effective agonist of μ opioid receptors, and has analgesic and respiratory depression effects. Ki is 12 nM.
CAT No: R1816
CAS No:88377-68-8
Synonyms/Alias:adrenorphin;Metorphamide;88377-68-8;HY-P1087;MFCD00065523;Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-NH2;DA-65420;MS-31834;H-Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-NH2;CS-0027637;Metorphamide; Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-NH2;(S)-N-((S)-1-amino-3-methyl-1-oxobutan-2-yl)-2-((2S,5S,8S,17S)-17-amino-8-benzyl-2-(3-guanidinopropyl)-18-(4-hydroxyphenyl)-5-(2-(methylthio)ethyl)-4,7,10,13,16-pentaoxo-3,6,9,12,15-pentaazaoctadecanamido)-5-guanidinopentanamide;
Adrenorphin is an endogenous peptide belonging to the opioid peptide family, characterized by its unique sequence and affinity for specific opioid receptors. As a naturally occurring neuropeptide, adrenorphin is derived from the proteolytic processing of proenkephalin A and is found in various tissues, including the adrenal medulla and central nervous system. Its biochemical significance is rooted in its modulatory effects on neurotransmission, neuroendocrine signaling, and its potential role in the regulation of stress and pain pathways. The study of adrenorphin has garnered interest in both fundamental neuroscience and peptide biochemistry, offering valuable insights into the complex interplay between peptide signaling and physiological homeostasis.
Neuropharmacology research: Adrenorphin serves as a critical tool for investigating the mechanisms of opioid receptor activation and downstream signaling pathways. By acting as a selective ligand for certain opioid receptors, it enables researchers to delineate the molecular interactions that underlie synaptic modulation, analgesic responses, and neuromodulatory effects. Utilizing this peptide in receptor binding assays, electrophysiological studies, or signaling cascade analyses allows for precise characterization of receptor subtype specificity and functional outcomes, advancing the understanding of endogenous opioid systems.
Peptide structure-activity relationship studies: The unique amino acid sequence and conformational properties of adrenorphin make it an ideal model for exploring structure-activity relationships (SAR) within the opioid peptide family. Through systematic modification, truncation, or labeling of the peptide, researchers can map critical residues responsible for receptor affinity and biological activity. These SAR investigations inform the rational design of synthetic peptide analogs with tailored pharmacological profiles, supporting the development of novel research tools and potential therapeutic leads in the field of peptide science.
Neuroendocrine signaling investigations: As a neuropeptide with established expression in the adrenal medulla and brain, adrenorphin provides a valuable system for studying the regulation of neuroendocrine axes. Experimental applications include examining its effects on hormone secretion, stress response modulation, and feedback mechanisms within the hypothalamic-pituitary-adrenal (HPA) axis. By leveraging in vitro and ex vivo models, scientists can dissect the peptide's influence on neuroendocrine cell signaling, contributing to a deeper understanding of peptide-mediated homeostatic regulation.
Peptide synthesis and analytical validation: The defined sequence and biological relevance of adrenorphin render it a useful standard in peptide synthesis protocols and analytical method development. It can be employed for validating chromatographic separation techniques, mass spectrometry calibration, and quality assessment of synthetic peptide preparations. Its use as a reference compound ensures reproducibility and accuracy in laboratory workflows, supporting robust peptide research and production methodologies.
Receptor-ligand interaction modeling: Adrenorphin's well-characterized receptor interactions make it suitable for computational modeling and molecular docking studies. By serving as a prototype ligand in in silico simulations, it aids in the elucidation of binding site architecture, conformational dynamics, and energetics of peptide-receptor complexes. These computational approaches complement experimental findings, providing a comprehensive framework for understanding opioid peptide recognition and informing the rational design of new bioactive molecules.
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