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 is an endogenous pentapeptide with significant biochemical interest due to its role as a natural inhibitor of enkephalin-degrading enzymes, including neutral endopeptidase (NEP) and aminopeptidase N (APN). Structurally composed of the amino acid sequence Gln-Arg-Phe-Ser-Arg, this peptide has attracted attention in neurobiology and pain modulation research for its ability to enhance the activity of endogenous enkephalins. Its unique mechanism of action, distinct from classical opioid compounds, positions it as a valuable molecular tool for dissecting the physiological regulation of pain pathways and neuropeptide signaling. Opiorphin's stability, bioactivity, and selectivity make it a versatile compound for a range of experimental applications in peptide biochemistry and neuroscience.
Neuropeptide research: As a potent modulator of enkephalin metabolism, opiorphin is widely utilized in studies investigating the regulation and function of endogenous opioid peptides in the central and peripheral nervous systems. By inhibiting the enzymatic breakdown of enkephalins, it enables researchers to probe the physiological roles of these neuropeptides in synaptic transmission, pain perception, and emotional processing. Its use facilitates the exploration of non-classical opioid pathways, providing insights into the broader landscape of neuropeptide-mediated signaling.
Enzyme inhibition assays: The compound serves as a reference inhibitor in biochemical assays designed to characterize the activity and specificity of neutral endopeptidase and aminopeptidase N. By acting as a competitive substrate or inhibitor, opiorphin allows for the quantitative assessment of enzyme kinetics, substrate preferences, and the efficacy of novel peptidase inhibitors. These studies are fundamental for understanding the molecular determinants of peptide degradation and for the development of new tools targeting peptidase activity.
Pain mechanism studies: Due to its capacity to potentiate endogenous enkephalin signaling, opiorphin is frequently employed in experimental models aimed at elucidating the molecular mechanisms underlying nociception and pain modulation. Researchers utilize the peptide to investigate the interplay between peptidase activity, opioid receptor signaling, and pain threshold regulation. Such studies contribute to a deeper understanding of the endogenous analgesic systems and may inform the design of future research into pain management strategies.
Peptide stability and pharmacokinetics: Investigators use opiorphin as a model peptide to study the factors influencing peptide stability, bioavailability, and metabolic fate in biological systems. Its susceptibility to enzymatic degradation and its interactions with plasma proteins make it an informative probe for evaluating peptide half-life, tissue distribution, and clearance rates. These parameters are critical for optimizing the design of peptide-based bioactive molecules and for advancing peptide delivery technologies.
Analytical method development: The unique sequence and biochemical properties of opiorphin make it a valuable standard in the development and validation of analytical techniques for peptide detection and quantification. Researchers employ it in the optimization of chromatographic, mass spectrometric, and immunoassay platforms, enabling the accurate measurement of low-abundance peptides in complex biological matrices. These methodological advancements support a wide array of applications in neurochemistry, biomarker discovery, and peptide therapeutics research.
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
4. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
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