Opiorphin is a naturally occurring pentapeptide that modulates peptidase activity in biochemical models. Its sequence displays a combination of polar and hydrophobic residues that influence stability and binding to metalloenzymes. Researchers employ it to explore endogenous peptidase regulation and substrate competition. Applications include enzymatic-pathway elucidation, peptide-stability research, and bioactive fragment characterization.
CAT No: R2579
CAS No:864084-88-8
Synonyms/Alias:Opiorphin;864084-88-8;L-Glutaminyl-L-arginyl-L-phenylalanyl-L-seryl-L-arginine;(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2,5-diamino-5-oxopentanoyl]amino]pentanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]amino]pentanoic acid;CHEMBL2022225;Opiorphin trifluoroacetate salt;Opiorphin?;QRFSR peptide;MFCD09752700;Gln-Arg-Phe-Ser-Arg;H-Gln-Arg-Phe-Ser-Arg-OH;SCHEMBL20257129;GTPL11538;CHEBI:177467;BDBM50382499;AKOS037646654;HY-W345510;AS-70071;DA-76445;FO109858;CS-0456478;glutaminyl-arginyl-phenylalanyl-seryl-arginine;D93123;Q416529;
Opiorphin, a naturally occurring pentapeptide, has garnered significant attention in scientific research due to its unique ability to modulate endogenous pain pathways and influence various physiological processes. Characterized by its origin in human saliva and remarkable stability against enzymatic degradation, Opiorphin demonstrates a novel mechanism of action by inhibiting specific enkephalin-degrading enzymes. This property allows for the potentiation of enkephalin-mediated signaling, thereby enhancing the body's natural ability to manage pain and stress. The peptide's multifaceted biological activities have positioned it as a valuable tool for researchers exploring neurobiology, pain modulation, and the intricate balance of neurotransmitter systems. Its ease of synthesis and compatibility with a range of experimental protocols further support its widespread adoption in laboratory investigations.
Neuroscience Research: In neuroscience, Opiorphin serves as an essential probe for elucidating the mechanisms underlying endogenous opioid pathways. By preventing the breakdown of enkephalins, it enables researchers to study the physiological consequences of sustained opioid receptor activation without the confounding effects associated with exogenous opioid administration. This approach is instrumental in dissecting the roles of specific opioid receptors in pain perception, emotional regulation, and reward circuits. The peptide's selectivity for enkephalinase enzymes provides a targeted means to explore the complex interplay between neuropeptides and neurotransmitters, advancing our understanding of the molecular basis of pain and mood disorders.
Pain Pathway Investigation: As a potent enkephalinase inhibitor, Opiorphin is frequently employed in experimental models to investigate endogenous pain control systems. Researchers utilize it to simulate conditions of heightened enkephalin availability, thereby mimicking natural analgesic responses. Through in vitro and in vivo studies, the peptide facilitates the mapping of pain transmission pathways and the identification of key molecular players involved in nociception. Its utility extends to the evaluation of novel analgesic compounds, where it serves as a reference standard for comparing the efficacy of other enkephalinase inhibitors or opioid-related agents.
Stress and Emotional Regulation Studies: The influence of Opiorphin on emotional states and stress responses represents another prominent area of application. By enhancing enkephalin-mediated signaling, it allows for the exploration of neurochemical pathways implicated in stress adaptation and emotional resilience. Researchers employ the peptide to examine behavioral and biochemical changes in response to stressors, providing insights into the neurobiological substrates of anxiety and depression. Its ability to modulate affective states without directly activating opioid receptors distinguishes it from traditional pharmacological agents and supports its use in preclinical models of mood disorders.
Pharmacological Screening: The peptide also finds utility in pharmacological screening platforms aimed at identifying and characterizing new modulators of enkephalinase activity. By serving as a benchmark inhibitor, Opiorphin enables the comparative analysis of candidate compounds for potency, selectivity, and mechanism of action. This application is particularly valuable in early-stage drug discovery, where it aids in the prioritization of hits and the optimization of lead molecules targeting the enkephalinergic system. Its well-characterized pharmacodynamic profile streamlines assay development and supports high-throughput screening initiatives.
Molecular Mechanism Elucidation: In the realm of molecular biology, Opiorphin is employed to dissect the enzymatic pathways responsible for enkephalin degradation. Its specificity for neprilysin and aminopeptidase N provides a unique tool for studying the structural and functional dynamics of these enzymes. Researchers leverage the peptide to investigate substrate-enzyme interactions, catalytic mechanisms, and the effects of genetic or pharmacological modulation on enkephalin turnover. Such studies contribute to a deeper understanding of peptide metabolism and inform the rational design of novel inhibitors with improved selectivity and efficacy.
Behavioral Pharmacology: In behavioral pharmacology, the use of Opiorphin facilitates the assessment of endogenous opioid system involvement in various behavioral paradigms. By modulating enkephalin levels, it allows for the evaluation of pain thresholds, reward sensitivity, and adaptive responses to environmental stimuli. Studies employing the peptide have shed light on the role of enkephalinase inhibition in shaping behavioral outcomes, providing a foundation for future investigations into the therapeutic potential of targeting endogenous opioid pathways. The versatility and specificity of Opiorphin make it an indispensable resource for advancing research in neurobiology, pharmacology, and peptide science.
4. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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