[Met5]-Enkephalin, amide is an agonist for δ opioid receptors as well as putative ζ (zeta) opioid receptors.
CAT No: R1125
CAS No:60117-17-1
Synonyms/Alias:Met-enkephalinamide;60117-17-1;[Met5]-Enkephalin, amide;Enkephalinamide-met-;H-Tyr-Gly-Gly-Phe-Met-NH2;[Met5]-Enkephalin Amide;CHEMBL247368;(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylsulfanylbutanamide;Tyr-Gly-Gly-Phe-Met-NH2;(S)-2-((S)-2-(2-(2-((S)-2-amino-3-(4-hydroxyphenyl)propanamido)acetamido)acetamido)-3-phenylpropanamido)-4-(methylthio)butanamide;[Met5]enkephalin amide;Methionine enkephalinamide;L-Methioninamide, L-tyrosylglycylglycyl-L-phenylalanyl-;DTXSID00975547;HY-P1467;BDBM50207823;DA-69332;CS-0044396;14-Amino-5-benzyl-4,7,10,13-tetrahydroxy-15-(4-hydroxyphenyl)-2-[2-(methylsulfanyl)ethyl]-3,6,9,12-tetraazapentadeca-3,6,9,12-tetraen-1-imidic acid;
[Met5]-Enkephalin, amide is a synthetic pentapeptide belonging to the enkephalin family, which are endogenous opioid peptides involved in modulating pain, mood, and various neurophysiological processes. Structurally characterized by its methionine residue at the fifth position and amidated C-terminus, [Met5]-Enkephalin, amide is widely recognized for its role as a natural ligand for opioid receptors, especially the delta and mu subtypes. Its defined sequence and stability make it a valuable tool in neurobiological, pharmacological, and biochemical research aimed at understanding opioid signaling pathways and peptide-receptor interactions.
Opioid receptor research: As a potent and selective agonist for delta and mu opioid receptors, [Met5]-Enkephalin, amide is extensively utilized in studies investigating the molecular mechanisms of opioid receptor activation, signal transduction, and downstream effects. Its defined structure enables precise mapping of receptor-ligand interactions, facilitating the elucidation of binding affinities, receptor conformational changes, and the structural basis for subtype selectivity. Researchers employ this peptide to dissect the pharmacodynamics of endogenous opioid systems in neural tissue and heterologous expression systems.
Neuropharmacology and synaptic modulation: The peptide serves as a critical probe in neuropharmacological studies exploring the modulation of synaptic transmission and neuronal excitability. By applying [Met5]-Enkephalin, amide to in vitro or ex vivo preparations such as brain slices and cultured neurons, investigators can assess its effects on neurotransmitter release, postsynaptic responses, and neuronal circuit dynamics. Such applications are instrumental in unraveling the physiological roles of enkephalins in pain perception, reward pathways, and neuroadaptive processes.
Peptide-receptor binding assays: [Met5]-Enkephalin, amide is frequently employed as a reference ligand in radioligand binding assays, fluorescence polarization, and surface plasmon resonance studies. Its high receptor affinity and well-characterized pharmacological profile make it an ideal standard for quantifying opioid receptor densities, evaluating receptor-ligand kinetics, and screening novel opioid modulators. These assays contribute to the development of new pharmacological agents targeting the opioid system and support structure-activity relationship analyses.
Peptide stability and degradation studies: Due to its susceptibility to enzymatic cleavage by peptidases such as enkephalinases, this peptide is a valuable substrate in research focused on peptide metabolism and degradation pathways. By monitoring the breakdown of [Met5]-Enkephalin, amide in biological matrices, scientists can characterize the activity of peptidases, investigate the regulation of endogenous peptide signaling, and assess the efficacy of enzyme inhibitors. These studies have broad implications for understanding peptide turnover and the modulation of neuropeptide signaling.
Peptide synthesis and analytical method development: The well-defined sequence and functional relevance of [Met5]-Enkephalin, amide render it a useful standard in the optimization of solid-phase peptide synthesis protocols and analytical techniques such as high-performance liquid chromatography and mass spectrometry. Researchers utilize it to validate synthetic methodologies, calibrate instrumentation, and establish protocols for the purification and characterization of opioid peptides. Its application in these contexts supports advances in peptide chemistry and quality control within research and industrial settings.
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