Deltorphin is a peptide enriched in aromatic and acidic residues, forming motifs that influence helix-loop transitions. The sequence supports research into receptor-like recognition, hydrophobic clustering, and solvent-dependent conformations. Researchers use it to study packing interactions and backbone dynamics. Its defined architecture aids rigorous biophysical profiling.
CAT No: R2237
CAS No:119975-64-3
Synonyms/Alias:Deltorphin;119975-64-3;Dermenkephalin;Deltorphin A;L-alpha-Asparagine, L-tyrosyl-D-methionyl-L-phenylalanyl-L-histidyl-L-leucyl-L-methionyl-;Tyr-met-phe-his-leu-met-asp-NH2;CHEMBL20775;CHEBI:81455;DTXSID60152630;Tyrosyl-methionyl-phenylalanyl-histidyl-leucyl-methionyl-aspartamide;(3S)-4-amino-3-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoyl]amino]-4-methylsulfanylbutanoyl]amino]-4-oxobutanoic acid;(5R,8S,11S,14S,17S,20S)-11-((1H-imidazol-4-yl)methyl)-5-((S)-2-amino-3-(4-hydroxyphenyl)propanamido)-8-benzyl-20-carbamoyl-14-isobutyl-17-(2-(methylthio)ethyl)-6,9,12,15,18-pentaoxo-2-thia-7,10,13,16,19-pentaazadocosan-22-oic acid;L-alpha-Asparagine, N2-(N-(N-(N-(N-(N-L-tyrosyl-D-methionyl)-L-phenylalanyl)-L-histidyl)-L-leucyl)-L-methionyl)-;H-Tyr-D-Met-Phe-His-Leu-Met-Asp-NH2;DTXCID3075121;GLXC-25917;3-(2-{2-[2-(2-{2-[2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-4-methylsulfanyl-butyrylamino}-3-phenyl-propionylamino)-3-(3H-imidazol-4-yl)-propionylamino]-4-methyl-pentanoylamino}-4-methylsulfanyl-butyrylamino)-succinamic acid;BDBM50000518;AKOS037647558;AKOS040744531;AS-74086;DA-72655;H-Tyr-(D)Met-Phe-His-Leu-Met-Asp-NH2;HY-129271;CS-0104599;C18010;G77949;Q5254878;3-(2-{2-[2-(2-{2-[2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-4-methylsulfanyl-butyrylamino}-3-phenyl-propionylamino)-3-(3H-imidazol-4-yl)-propionylamino]-4-methyl-pentanoylamino}-4-methylsulfanyl-butyrylamino)-succinamic acid (deltorphin A);
Deltorphin is a naturally occurring heptapeptide belonging to the class of opioid peptides, originally isolated from the skin of certain amphibian species. Distinguished by its high affinity and exceptional selectivity for the delta-opioid receptor, deltorphin plays a significant role in the study of endogenous opioid systems and receptor pharmacology. Its unique structure and receptor-binding profile make it a valuable tool for elucidating the physiological and biochemical mechanisms underlying pain modulation, mood regulation, and receptor-ligand interactions within the central nervous system. As a research peptide, deltorphin is widely recognized for its utility in advancing understanding of opioid receptor biology and supporting the development of selective receptor assays.
Receptor Pharmacology: Deltorphin is extensively utilized in research focused on delta-opioid receptor pharmacology. Due to its pronounced selectivity and binding affinity, the peptide serves as a robust ligand for characterizing receptor subtypes, mapping receptor distribution, and evaluating receptor-ligand interactions in both in vitro and ex vivo systems. Studies employing deltorphin enable researchers to dissect the structural and functional differences between opioid receptor families, providing insights that are critical for the rational design of receptor-specific probes and modulators.
Signal Transduction Studies: In the context of intracellular signaling, deltorphin is a preferred tool for probing the downstream effects of delta-opioid receptor activation. By engaging these receptors, the peptide facilitates the examination of G-protein coupled receptor (GPCR) signaling cascades, second messenger systems, and regulatory feedback mechanisms. This application is particularly valuable for elucidating the molecular basis of receptor-mediated neurochemical responses and for identifying potential targets for pharmacological intervention in neurological research.
Peptide Structure-Activity Relationship (SAR) Analysis: The structural features of deltorphin, including its amino acid sequence and conformational properties, make it an important model for peptide structure-activity relationship studies. Researchers employ synthetic analogs and modifications of deltorphin to investigate how specific residues and sequence motifs influence receptor binding, selectivity, and biological activity. These SAR investigations contribute to the broader understanding of peptide-receptor interactions and inform the design of novel opioid peptides with tailored pharmacological profiles.
Assay Development: Deltorphin is frequently incorporated into the development and validation of bioassays targeting delta-opioid receptors. Its high specificity and potency allow for the establishment of sensitive and reliable assay systems, such as radioligand binding assays, fluorescence-based detection methods, and functional activity screens. These assays are instrumental in screening for new delta-opioid ligands, characterizing receptor antagonists or agonists, and quantifying receptor expression in various biological samples.
Neuroscience Research: The unique pharmacological characteristics of deltorphin have positioned it as a key reagent in neuroscience investigations exploring endogenous opioid functions. Researchers utilize the peptide to study neural circuits involved in nociception, emotional regulation, and synaptic plasticity. By selectively activating delta-opioid pathways, deltorphin enables the dissection of receptor-specific contributions to complex neurobiological processes, fostering a deeper understanding of the physiological roles of opioid peptides in the brain and peripheral nervous system.
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