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Dermorphin Sale

(Synonyms: 皮啡肽) 目录号 : GC31168

An opioid peptide

Dermorphin Chemical Structure

Cas No.:77614-16-5

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实验参考方法

Kinase experiment:

Membrane protein (40 μg) is incubated in 0.5 mL volume of 50 mM Tris, 0.2 mM EGTA, 1 mM MgCl2, 100 mM NaCl, 0.1% BSA, 0.15 mM bacitracin; pH 7.4, GDP (33 μM), and ∼150 pM GTPγ[35S]. Varying concentrations of reference ligands (Dermorphin, N/OFQ, Dynorphin-A and Leu-enkephalin) or DeNo (1 pM-10 μM) is added prior to incubation. Non-specific binding is determined in the presence of unlabeled GTPγS (10 μM). Samples are incubated at 30°C for 1 h with gentle agitation. Reactions are terminated by vacuum filtration through dry Whatman GF/B filters, using a Brandel harvester[2].

References:

[1]. Tiwari V, et al. Activation of Peripheral μ-opioid Receptors by Dermorphin [D-Arg2, Lys4] (1-4) Amide Leads to Modality-preferred Inhibition of Neuropathic Pain. Anesthesiology. 2016 Mar;124(3):706-20.
[2]. Bird MF, et al. Characterisation of the Novel Mixed Mu-NOP Peptide Ligand Dermorphin-N/OFQ (DeNo). PLoS One. 2016 Jun 7;11(6):e0156897.

产品描述

Dermorphin is an opioid peptide originally isolated from the skin of South American frogs (Ph. sauvagei).1 It binds to μ-opioid receptors (Ki = 0.54 nM) and is selective for μ- over δ-opioid receptors in radioligand binding assays (Ki = 929 nM). In vivo, dermorphin (1.9 ?mol/kg, i.p.) inhibits noxious stimuli-induced neuronal firing in the nucleus lateralis anterior and ventrobasal complex in rats.2 It inhibits the electrical stimulation-induced C fiber response in rat dorsal horn nociceptive neurons. Dermorphin (10-120 pmol/animal, i.c.v.) delays gastric emptying, inhibits gastric acid secretion, and slows colonic motility in pylorus-ligated rats.

1.Usenko, A.B., Emel'yanova, T.G., and MIasoedov, N.F.Dermorphins are natural opioids with an unique primary structure that determines their biological specificityBiol. Bull. Russ. Acad. Sci.29154-164(2002) 2.Melchiorri, P., and Negri, L.The dermorphin peptide familyGen. Pharmacol.27(7)1099-1107(1996)

Chemical Properties

Cas No. 77614-16-5 SDF
别名 皮啡肽
Canonical SMILES Tyr-{d-Ala}-Phe-Gly-Tyr-Pro-Ser-NH2
分子式 C40H50N8O10 分子量 802.87
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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1 mM 1.2455 mL 6.2277 mL 12.4553 mL
5 mM 0.2491 mL 1.2455 mL 2.4911 mL
10 mM 0.1246 mL 0.6228 mL 1.2455 mL
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Research Update

The dermorphin peptide family

1. In 1980, the skin of certain frogs belonging to the genus Phyllomedusinae was found to contain two new peptides that proved to be selective mu-opioid agonists. Given the name dermorphins, these were the first members of a peptide family that in the past 15 years has grown to reach a total of seven naturally occurring peptides and nearly 30 synthetic analogs. 2. Dermorphin peptides are potent analgesics in rodents and primates, including man. Some dermorphins can enter the blood-brain barrier and produce central antinociception after peripheral administration. 3. The dermorphin family also includes mu 1-opioid receptor selective agonists that produce intense opioid analgesia, but stimulate pulmonary ventilation. 4. Experiments in rats and mice chronically exposed to dermorphins have shown that not only do they have higher antinociceptive efficacy and potency than morphine, but they are also less likely than morphine to produce tolerance, dependence and opiate side effects.

Dermorphin tetrapeptide analogs as potent and long-lasting analgesics with pharmacological profiles distinct from morphine

Dermorphin (Tyr-d-Ala-Phe-Gly-Tyr-Pro-Ser-NH(2)) is a heptapeptide isolated from amphibian skin. With a very high affinity and selectivity for μ-opioid receptors, dermorphin shows an extremely potent antinociceptive effect. The structure-activity relationship studies of dermorphin analogs clearly suggest that the N-terminal tetrapeptide is the minimal sequence for agonistic activity at μ-opioid receptors, and that the replacement of the d-Ala(2) residue with d-Arg(2) makes the tetrapeptides resistant to enzymatic metabolism. At present, only a handful of dermorphin N-terminal tetrapeptide analogs containing d-Arg(2) have been developed. The analogs show potent antinociceptive activity that is greater than that of morphine with various injection routes, and retain high affinity and selectivity for μ-opioid receptors. Interestingly, some analogs show pharmacological profiles that are distinct from the traditional μ-opioid receptor agonists morphine and [d-Ala(2),NMePhe(4),Gly-ol(5)]enkephalin (DAMGO). These analogs stimulate the release of dynorphins through the activation of μ-opioid receptors. The activation of κ-opioid receptors by dynorphins is suggested to reduce the side effects of μ-opioid receptor agonists, e.g., dependence or antinociceptive tolerance. The dermorphin N-terminal tetrapeptide analogs containing d-Arg(2) may provide a new target molecule for developing novel analgesics that have fewer side effects.

Rediscovery of old drugs: the forgotten case of dermorphin for postoperative pain and palliation

The repurposing of old drugs for new indications is becoming more accepted as a cost-efficient solution for complicated health problems. However, older drugs are often forgotten when they are not repositioned. This analysis makes a case for re-exploration of dermorphin for intrathecal use in postoperative pain and in a palliative context, with the goal of re-establishing this compound. Dermorphin was isolated from the skin of an Amazonian frog, characterized and identified as a bioactive heptapeptide by Vittorio Erspamer's research group in the early 1980s. It was traditionally called "Kambo" or "Sapo" by Amazon tribes and was used to improve their physical and psychic skills as hunters. Its structure is rather enigmatic, containing a D-amino acid, and its pharmacological activity in a number of assays was found to be quite impressive and superior to morphine. Moreover, it has been established as more selective and potent with long-lasting analgesia compared to morphine after intracerebroventricular administration in animal models. In 1985, the first clinical trial results of a randomized, placebo-controlled study in postoperative pain were reported, and dermorphin administered via the intrathecal route was again impressively superior over the placebo and the reference compound morphine. This milestone study was apparently minimally read by clinicians, as the study has never been referenced; only 15 pharmacological and review papers after 1985 mentioned the results, with not one being a clinical paper. The interest in dermorphin decreased after 1985, and the compound was never again introduced in the clinical setting. Considering the enormous pressure to find superior acting opioids, this is quite puzzling. We suggest new clinical studies to further evaluate the safety and efficacy of dermorphin, especially administered via the intrathecal route in postoperative pain or for palliative use in terminal patients.

Evaluation of Dermorphin Metabolism Using Zebrafish Water Tank Model and Human Liver Microsomes

Background: Dermorphin is a heptapeptide with an analgesic potential higher than morphine that does not present the same risk for the development of tolerance. These pharmacological features make dermorphin a potential doping agent in competitive sports and it is already prohibited for racehorses. For athletes, the development of an efficient strategy to monitor for its abuse necessitates an investigation of the metabolism of dermorphin in humans.
Methods: Here, human liver microsomes and zebrafish were utilized as model systems of human metabolism to evaluate the presence and kinetics of metabolites derived from dermorphin. Five hours after its administration, the presence of dermorphin metabolites could be detected in both models by liquid chromatography coupled to highresolution mass spectrometry.
Results: Although the two models showed common results, marked differences were also observed in relation to the formed metabolites. Six putative metabolites, based on their exact masses of m/z 479.1915, m/z 501.1733, m/z 495.1657, m/z 223.1073, m/z 180.1017 and m/z 457.2085, are proposed to represent the metabolic pattern of dermorphin. The major metabolite generated from the administration of dermorphin in both models was YAFG-OH (m/z 457.2085), which is the N-terminal tetrapeptide previously identified from studies on rats.
Conclusion: Its extensive characterization and commercial availability suggest that it could serve as a primary target analyte for the detection of dermorphin misuse. The metabolomics approach also allowed the assignment of other confirmatory metabolites.

Pharmacokinetics and pharmacodynamics of dermorphin in the horse

Dermorphin is a μ-opioid receptor-binding peptide that causes both central and peripheral effects following intravenous administration to rats, dogs, and humans and has been identified in postrace horse samples. Ten horses were intravenously and/or intramuscularly administered dermorphin (9.3 ± 1.0 μg/kg), and plasma concentration vs. time data were evaluated using compartmental and noncompartmental analyses. Data from intravenous administrations fit a 2-compartment model best with distribution and elimination half-lives (harmonic mean ± pseudo SD) of 0.09 ± 0.02 and 0.76 ± 0.22 h, respectively. Data from intramuscular administrations fit a noncompartmental model best with a terminal elimination half-life of 0.68 ± 0.24 (h). Bioavailability following intramuscular administration was variable (47-100%, n = 3). The percentage of dermorphin excreted in urine was 5.0 (3.7-10.6) %. Excitation accompanied by an increased heart rate followed intravenous administration only and subsided after 5 min. A plot of the mean change in heart rate vs. the plasma concentration of dermorphin fit a hyperbolic equation (simple Emax model), and an EC(50) of 21.1 ± 8.8 ng/mL was calculated. Dermorphin was detected in plasma for 12 h and in urine for 48 or 72 h following intravenous or intramuscular administration, respectively.