Dalargin (DALE) has originally been proposed as an antiulcer agent with cytoprotective properties; but it has been tested for other activities with promising results. Dalargin shows antioxidant; antiischemic; and wound-healing properties.
CAT No: HB00104
CAS No:81733-79-1
Synonyms/Alias:Dalargin;81733-79-1;Enkephalin-leu, ala(2)-arg(6)-;2-Ala-6-Arg-Leu-enkephalin;DALARGINE;(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid;UNII-V13505565P;DALARGIN [WHO-DD];BRN 4287455;Tyr-D-Ala-Gly-Phe-Leu-Arg;2-D-Alanine-1-6-beta-neoendorphin (human);DTXSID50231302;1-6-(D-ALA2)-DYNORPHIN;Tyrosyl-D-alanyl-glycyl-phenylalanyl-leucyl-arginine;tageflar;V13505565P;1-6-beta-Neoendorphin (human), 2-D-alanine-;N(sup 2)-(N-(N-(N-(L-Tyrosyl-D-alanyl)glycyl)-L-phenylalanyl)-L-leucyl)-L-arginine;1-6-.BETA.-NEOENDORPHIN (HUMAN), 2-D-ALANINE-;L-ARGININE, L-TYROSYL-D-ALANYLGLYCYL-L-PHENYLALANYL-L-LEUCYL-;L-Arginine, N(sup 2)-(N-(N-(N-(L-tyrosyl-D-alanyl)glycyl)-L-phenylalanyl)-L-leucyl)-;Tyr-Ala-Gly-Phe-Leu-Arg;Leu-enkephalin, Ala(2)-Arg(6)-;leucine-enkephalin, Ala(2)-Arg(6)-;enkephalin, Ala(2)-Leu(5)-Arg(6)-;enkephalin-Leu, alanyl(2)-arginine(6)-;(D-Ala2)-Leu-Enkephalin-Arg acetate salt;tyrosyl-alanyl-glycyl-phenylalanyl--leucyl-arginine;DTXCID10153793;EX-A5715;H-Tyr-D-Ala-Gly-Phe-Leu-Arg-OH;HY-P4053;FA108952;CS-0635584;Q27291394;(2S,5S,8S,14R,17S)-17-amino-8-benzyl-2-(3-guanidinopropyl)-18-(4-hydroxyphenyl)-5-isobutyl-14-methyl-4,7,10,13,16-pentaoxo-3,6,9,12,15-pentaazaoctadecan-1-oic acid;
DALARGIN is a synthetic hexapeptide belonging to the enkephalin class of opioid peptides, distinguished by its unique amino acid sequence and potent biological activities. As a laboratory reagent, DALARGIN demonstrates high solubility in aqueous solutions and exhibits notable stability under standard storage conditions, making it a reliable choice for experimental protocols. Its structural resemblance to endogenous opioid peptides allows it to interact selectively with opioid receptors, particularly those in the central nervous system and peripheral tissues. Researchers value DALARGIN for its reproducibility in in vitro and in vivo studies, as well as its ability to modulate a range of physiological responses. The versatility of this compound has prompted widespread investigation across multiple scientific fields, including neurobiology, pharmacology, and peptide chemistry, where it serves as a valuable reference and experimental tool in elucidating peptide-receptor interactions and signaling pathways.
Neuroscience research: DALARGIN is extensively utilized in neuroscience research to probe the mechanisms of pain modulation and neuroprotection. Its activity at opioid receptors enables scientists to study the signaling cascades involved in analgesia, stress response, and synaptic plasticity. By applying DALARGIN in neuronal cell cultures or animal models, researchers can dissect the downstream effects of opioid receptor activation, including alterations in neurotransmitter release and gene expression. Such studies are critical for understanding the molecular underpinnings of pain perception and the development of novel therapeutics targeting the opioid system.
Pharmacological studies: In pharmacological investigations, DALARGIN serves as a model compound for evaluating the efficacy and specificity of opioid receptor agonists. Its well-characterized profile allows for the assessment of receptor binding affinities, dose-response relationships, and competitive interactions with other ligands. By comparing DALARGIN's effects with those of other synthetic or natural peptides, researchers can identify structure-activity relationships and optimize the design of new opioid analogs. These studies contribute to the broader understanding of opioid pharmacodynamics and the potential for developing compounds with improved safety and efficacy profiles.
Peptide-receptor interaction assays: The application of DALARGIN in peptide-receptor interaction assays is instrumental for mapping receptor subtypes and elucidating binding domains. Using advanced techniques such as radioligand binding, surface plasmon resonance, and fluorescence resonance energy transfer, scientists can quantify the affinity and kinetics of DALARGIN's interaction with different opioid receptors. These assays help clarify the molecular determinants of receptor selectivity and inform the rational design of peptide-based probes or therapeutics. The insights gained from such studies are pivotal for advancing receptor biology and developing targeted interventions.
Biochemical pathway elucidation: DALARGIN is also employed to investigate the modulation of intracellular signaling pathways downstream of opioid receptor engagement. Researchers use the peptide to monitor changes in second messenger systems, such as cyclic AMP or calcium flux, and to analyze the activation of kinases and transcription factors. Through these experiments, it becomes possible to delineate the cellular consequences of opioid receptor activation and to identify potential cross-talk with other signaling networks. Such knowledge is essential for understanding the broader physiological roles of opioid peptides and their impact on cellular homeostasis.
Peptide engineering and analog development: In the field of peptide engineering, DALARGIN acts as a template for the synthesis and evaluation of novel peptide analogs with modified pharmacological properties. By introducing strategic amino acid substitutions or chemical modifications, scientists can enhance the stability, receptor selectivity, or bioavailability of DALARGIN-based molecules. These engineered peptides are then tested in a variety of biological assays to determine their functional characteristics and therapeutic potential. The iterative process of analog development, guided by the properties of DALARGIN, accelerates the discovery of new peptide-based tools and candidates for further research.
Through its multifaceted applications, DALARGIN continues to be a cornerstone reagent in peptide science, facilitating advancements in neurobiology, pharmacology, receptor biology, and peptide engineering. The compound's robust performance in diverse experimental systems underscores its significance as an indispensable resource for researchers seeking to unravel the complexities of opioid signaling and peptide therapeutics.
2. TMEM16F and dynamins control expansive plasma membrane reservoirs
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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