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Dermorphin In Humans is a peptide compound composed of multiple amino acid residues, with a molecular formula of C40H50N8O10, CAS 77614-16-5, and a molecular weight of 802.87. The molecule contains multiple disulfide bonds, and the presence of these disulfide bonds gives the peptide a certain degree of rigidity and stability. Dermorphin peptide is soluble in organic solvents such as methanol, ethanol, acetone, ethyl acetate, chloroform, methyl ethyl ketone, and benzene, but not in water. This dissolution characteristic poses certain challenges for its preparation and purification. There is no obvious absorption peak in the visible light range, which is related to the absence of colored groups. It has a certain degree of stability at high temperatures, which gives it a certain degree of heat resistance during preparation, storage, and use. It has certain acid-base properties and has certain stability under acidic conditions, but may undergo decomposition or deterioration under alkaline conditions.
Package
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Chemical Formula |
C28H27NO4S |
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Exact Mass |
802.36 |
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Molecular Weight |
802.89 |
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m/z |
802.36 (100.0%), 803.37 (43.3%), 804.37 (9.1%), 803.36 (3.0%), 804.37 (2.1%), 804.37 (1.3%) |
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Elemental Analysis |
C, 59.84; H, 6.28; N, 13.96; O, 19.93 |
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Morphological |
Powder |
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Color |
White to off-white |
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Melting Point |
157 – 159 °C |
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Boiling Point |
1323.8 ± 65.0 ° C ( Predicted ) |
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Density |
1.363 ± 0.06 g / cm3 ( Predicted ) |
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Storage Conditions |
2-8 °C |
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Solubility Alcohol |
Solublesoluble 40 parts of solvent |
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Acidity Coefficient ( pKa ) |
83 ± 0.15 ( Predicted ) |
Customized Bottle Caps & Corks
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Synthesis Methods
Method 1: Solid phase peptide synthesis
The solid-phase peptide synthesis method is a commonly used laboratory synthesis method, which is based on the principle of synthesizing amino protected peptide chains on a solid-phase carrier to avoid difficulties in aggregation and separation during the synthesis process. This method includes the following steps:
Select suitable solid phase carriers such as polystyrene resin, polyethylene pyridine, etc., and fix amino acids protected by amino acids (such as Boc amino acids) onto the solid phase carrier using methods such as chloromethyl ether or dichloromethylsilane.
Add a solid phase carrier, organic solvent, and condensation agent (such as DIC/Oxyma) to the reactor, and then add carboxyl protected amino acids to react with the amino groups on the solid phase carrier to form peptide bonds.
Wash the reaction solution with anhydrous dichloromethane or n-hexane, and wash the peptide chain with a condensation agent or proton solvent. Repeat the above operation until the peptide chain synthesis is completed.
Use proton solvent to break down the peptide chain, and remove the protective group with dilute hydrochloric acid or alkali to obtain crude peptide.
Use chromatography to separate and purify the crude product, and obtain high-purity dermorphin.
Method 2: Biosynthetic
Biosynthesis is a method of producing peptide compounds using microorganisms or cells. This method typically utilizes the metabolic pathways of microorganisms or cells to produce target molecules, such as using microbial fermentation to produce antibiotics. The advantage of biosynthesis is that it can utilize the natural metabolic capacity of organisms to produce target molecules, but it requires controlling the growth conditions and metabolic pathways of microorganisms or cells.
Biosynthesis is a method of producing dermokinin using microorganisms or cells. This method typically utilizes the metabolic pathways of microorganisms or cells to produce target molecules, such as using microbial fermentation to produce antibiotics. The following are the detailed steps and chemical equations for the biosynthesis of corticorpin:
Strain selection: Select microorganisms or cells that can produce peptide as strains, such as molds, yeast, bacteria, etc.
Seed culture: Inoculate the selected strain into the seed culture medium for moderate cultivation and reproduction to obtain sufficient biomass.
Fermentation culture: Inoculate microorganisms or cells obtained from seed culture into fermentation medium, and carry out fermentation culture under suitable conditions to promote the production of corticorpin.
Extraction of Pikephalin: Pikephalin can be extracted from fermentation broth using physical methods (such as centrifugation, filtration), chemical methods (such as extraction, ion exchange), or biological methods (such as adsorption, precipitation).
Purification of Pikephalin: The extracted Pikephalin is purified by chromatography, precipitation, and other methods to obtain high-purity Pikephalin.
The following is a specific chemical equation for the biosynthesis of dermorphin:
Fermentation culture
CO ₂+H ₂ O+C3H7ClN2O2S → CHO-R+CO ₂+C3H7N+C10H15N5O10P2
Extraction and purification
CHO-R+H ₂ O → CHOH-R+C3H7N+C10H15N5O10P2
CHOH-R+H ₂ O → CH ₂ OH-R+C3H7N+C10H15N5O10P2
CH ₂ OH-R+H ₂ O → CH ₂ OHCH ₂ OH-R+C3H7N+C10H15N5O10P2
CH ₂ OHCH ₂ OH-R+H ₂ O → CH ₂ OHCH ₂ OHCH ₂ OH-R+C3H7N+C10H15N5O10P2
Dermorphin is one of opioids, which has strong analgesic activity. Dermorphin was first discovered from the skin of frogs in South America. Some peptides produced in vivo have similar physiological effects to morphine. However, the mechanism of dermorphin analgesia is still unclear.
Dermorphin In Humans is also widely used in the field of pharmacognosy. Pharmacognosy is a science that studies natural drugs, involving the discovery, identification, production, and application of drugs. Pikephalin, as a natural bioactive peptide, has multiple pharmacological effects and biological activities, making it widely applicable in pharmacognosy. The following are the various applications of corticosteroids in pharmacognosy:
As a natural product with multiple pharmacological effects and biological activities, corticorpin can be used as a candidate for drug development. In the process of drug discovery and identification, the chemical structure, biological activity, pharmacokinetic properties, and other aspects of corticorpin need to be studied and identified in detail. Through these studies, the efficacy and mechanism of action of corticorpin can be determined, providing scientific basis for subsequent drug development and production.
After determining the efficacy and mechanism of action of dermorphin, the field of pharmacognosy still needs to optimize its production process. This includes selecting suitable raw materials, optimizing extraction and separation methods, and improving production processes. By optimizing the production process, the production efficiency and product quality of opioid can be improved, production costs can be reduced, and better conditions can be provided for the production and application of drugs.
After determining the production process of dermorphin, the field of pharmacognosy requires drug production and quality control. This includes developing corresponding production processes and quality standards based on indicators such as the chemical structure, biological activity, and pharmacokinetic properties of dermorphin. Through these standards and regulations, the quality and stability of drugs can be guaranteed, and the safety and effectiveness of drugs can be ensured.
In the field of pharmacognosy, there is still a need to study the mechanism of drug action. This includes studying the ways in which corticorpins interact with targets, as well as their effects on various systems in the body. Through these studies, we can gain a deeper understanding of the efficacy and safety of drugs, providing theoretical basis for the improvement and optimization of drugs.
After completing the production and quality control of drugs, clinical trials and drug evaluation are required in the field of pharmacognosy. This includes evaluating the pharmacodynamics, pharmacokinetics, safety, and other aspects of corticorpin. Through these evaluations, a comprehensive understanding of the efficacy, safety, and adverse reactions of drugs can be obtained, providing scientific basis for their application.
Dermorphin In Humans, also known as its chemical name, is a naturally occurring heptapeptide μ-opioid receptor (MOR) agonist discovered in the skin of amphibians. Its CAS number is 77614-16-5, indicating its unique chemical identity. The peptide consists of seven amino acids with the sequence H2N-Tyr-DAla-Phe-Gly-Tyr-Pro-Ser-NH2, giving it a molecular formula of C40H50N8O10 and an average molecular weight of 802.87.
Dermorphin was originally isolated from the skin of a South American tree frog, highlighting its natural origin. This peptide exhibits strong analgesic properties due to its ability to activate μ-opioid receptors in the body, similar to the effects of morphine. However, the precise mechanism of its analgesic action remains unclear.
In addition to its natural occurrence, dermorphin can also be synthesized chemically for research purposes. It is commonly used in scientific studies due to its high purity (up to 99%) and specific biological activity. However, it is important to note that dermorphin is only intended for research and should not be used in humans.
The physical effects of dermorphin peptide on peptide chain dynamics
Dynamic control of charge distribution
Net charge and isoelectric point
The net charge of dermorphin is -1 (pH 7.4), and its isoelectric point is 5.8. Its charge distribution exhibits characteristics of negative charge at the N-terminus (dissociation of Tyr ¹'s phenolic hydroxyl group) and weak negative charge at the C-terminus (partial dissociation of Ser ⁷'s hydroxyl group). This charge distribution allows it to bind with plasma proteins (such as albumin, pI=4.7) in the blood through electrostatic interactions, prolonging the half-life to 20-30 hours (natural IGF-1 only takes 10-20 minutes).
pH dependent conformational changes
In acidic environments (such as lysosomes, pH 4.5), the phenolic hydroxyl protonation of Tyr ¹ leads to:
The hydrogen bond with D-Ala is broken, and the β - corner structure is loose;
Exposure of hydrophobic core promotes binding with receptors;
Reduce net charge to 0, decrease binding with plasma proteins, and enhance tissue permeability.
This pH dependent conformational change increases the analgesic activity of dermorphin by three times at the site of inflammation (pH decrease).
Biological functions of dynamic conformational changes
Conformation selection for receptor binding
The binding of dermorphin to the μ receptor follows a "conformational selection induced fit" mechanism:
Pre organized conformation: Dermorphin exists in an active conformation with N-terminal β - rotation and C-terminal random curling in solution;
Receptor screening: The receptor conformational pocket only accommodates specific conformations and excludes other low-energy states;
Induced binding: After binding, the side chain of Ser ⁷ rotates 120 ° and forms a new hydrogen bond with the receptor Glu ③¹⁰, stabilizing the complex.
This process results in a binding rate constant (k ₁) of 1.2 × 10 ⁸ M ⁻¹ s ⁻¹, much higher than morphine (3.5 × 10 ⁶ M ⁻¹ s ⁻¹).
Structural basis of enzymatic resistance
The resistance of dermorphin to peptidases originates from:
Stereoscopic shielding of D-Ala: The methyl group of D-Ala obstructs the approach of trypsin (cleavage of Lys/Arg-C end) and chymotrypsin (cleavage of aromatic residues - C end);
Compact structure: The β - angle makes the peptide chain spherical, reducing the contact area with the active center of the peptidase;
Charge distribution: Negative charges are concentrated at the N-terminus, repelling negatively charged peptidase surfaces.
Experiments have shown that the half-life of dermorphin in serum is 10 times that of natural opioid peptides.
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