Sermorelin powder is a synthetic Growth Hormone-Releasing Peptide (GHRP). The chemical formula is C149H246N44O42S, CAS 86168-78-7, and the molecular weight is 3357.88 g/mol. It consists of a polypeptide chain of 29 amino acid residues. It is a colorless or off-white powdery substance. High solubility in water. It can also be dissolved in some organic solvents such as ethanol. It is a growth hormone releasing peptide analogue, which is structurally similar to endogenous growth hormone releasing hormone (Growth Hormone-Releasing Hormone, referred to as GHRH). It consists of the first to second nine amino acid residues of GHRH with a D-glutamyl amino acid between the second and third residues. Relatively stable at room temperature. However, it may be degraded by factors such as light, heat and oxygen. In order to maintain its stability, it should be stored in a dry, dark and low temperature environment.
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Sermorelin COA
Customized Bottle Caps & Corks
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Chemical Formula |
C149H246N44O42S |
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Exact Mass |
3356 |
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Molecular Weight |
3358 |
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m/z |
3357 (100.0%), 3358 (80.0%), 3356 (62.1%), 3359 (35.2%), 3358 (16.3%), 3359 (13.0%), 3357 (10.1%), 3360 (10.0%), 3359 (8.6%), 3359 (7.3%), 3360 (6.9%), 3360 (6.7%), 3360 (5.7%), 3358 (5.4%), 3359 (4.5%), 3360 (3.6%), 3361 (3.2%), 3361 (3.0%), 3358 (2.8%), 3358 (2.8%), 3359 (2.3%), 3361 (2.1%), 3357 (1.8%), 3361 (1.6%), 3358 (1.6%), 3361 (1.6%), 3362 (1.4%), 3360 (1.4%), 3359 (1.3%), 3359 (1.3%), 3360 (1.2%), 3361 (1.1%), 3361 (1.1%), 3362 (1.0%), 3360 (1.0%) |
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Elemental Analysis |
C, 53.30; H, 7.38; N, 18.35; O, 20.01; S, 0.95 |
Structure & Molecular Characteristics
Peptide structure: Sermorelin is a polypeptide hormone consisting of 29 amino acid residues. Its chemical structure is similar to the N-terminal portion of the human endogenous growth hormone releasing hormone (GHRH).
Amino acid sequence: The amino acid sequence of Sermorelin is H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala- Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2. This sequence determines the biological activity and function of Sermorelin.
Amino acid inversion: Compared with the original GHRH, Sermorelin inverts the amino acid sequence. This inverted arrangement is to ensure that the polypeptide chains fold correctly and form biologically active structures.
Reactive residues: Each amino acid residue in Sermorelin has different reactivity. For example, the ε-hydroxyl group of lysine and the phenolic hydroxyl group of tyrosine can participate in the esterification reaction and the like.
Three-dimensional structure: The amino acid sequence of Sermorelin will form a specific three-dimensional structure under certain conditions. This structure is crucial for the biological activity and interaction of Sermorelin.
Acylation: In order to increase the stability and biological activity of Sermorelin, its C-terminal end is usually acylated. This treatment can be carried out under suitable conditions by using an appropriate acylating agent.
Overall, Sermorelin is a polypeptide hormone consisting of 29 amino acids, whose structure and amino acid sequence are similar to the N-terminal part of human endogenous GHRH. Its molecular features include amino acid inversions, reactive residues, three-dimensional structure, and acylation. These characteristics determine the biological activity and function of Sermorelin, making it an effective drug for stimulating growth hormone secretion.
Sermorelin powder is a synthetic growth hormone releasing peptide (Growth Hormone-Releasing Peptide, referred to as GHRP), which is mainly used to treat some diseases related to growth hormone deficiency.
Growth hormone deficiency treatment:
Growth hormone is an important hormone secreted by the pituitary gland to control human growth and metabolism. Growth hormone deficiency can lead to problems such as growth retardation and bone age delay in children, while it can cause metabolic abnormalities and cardiovascular diseases in adults. Sermorelin treats growth hormone deficiency by stimulating the release of growth hormone from the pituitary gland.
Treatment of short stature in children:
Short stature in children is defined as slow growth in children within the range of normal growth potential. Sermorelin can promote the growth and development of children and increase the rate of height growth. It supplements the lack of growth hormone by stimulating the pituitary gland to secrete growth hormone.
Reverse aging:
With age, the secretion of growth hormone in the human body gradually decreases. Such physiological changes are associated with various aging processes. Sermorelin is used by some as an antiaging treatment. By stimulating the pituitary gland to release more growth hormone, Sermorelin may help improve skin elasticity, increase muscle mass, reduce fat accumulation, and improve mental status and cognitive function.
Physical improvement:
Since Sermorelin increases muscle strength and mass, some fitness enthusiasts use it to improve body composition. In addition, Sermorelin can also promote sports rehabilitation and help recover after sports injuries or surgery.
Improve sleep quality:
Growth hormone is closely related to sleep. Sermorelin use may promote increased deep sleep and rapid eye movement (REM) sleep stages, resulting in improved sleep quality.
Enhanced performance:
Sermorelin is used by some sports athletes and fitness enthusiasts as a performance-enhancing supplement. It improves muscle strength, endurance and recovery, and promotes muscle growth and repair.
Treatment of other diseases:
Sermorelin is also used to treat some other diseases, such as endocrine disorders, low energy syndrome, chronic fatigue syndrome, etc. However, more research and clinical trial data are needed to support the therapeutic effects of these diseases.
Synthesis Methods
Prepare the required chemical reagents, solvents and equipment. These reagents may include protecting groups, activators, amino acids, organic solvents, etc.
First, a ChIP carrier is ligated to the starting amino acid. Chip supports often contain hydroxyl groups (eg, ethylparaben) that form ester bonds with amino acids.
Polypeptide chains are synthesized step-by-step on chip carriers using solid-phase synthesis technology. Each time an amino acid is added, the correct protecting group (to prevent reactions at other sites) and activator needs to be selected. The synthesis process usually employs precise time control and temperature conditions.
After the complete polypeptide chain has been synthesized, the protecting groups need to be removed to restore the amino acids to their free state. A common method is to use appropriate reagents and conditions (such as trifluoroacetic acid).
Synthetic polypeptide chains may be accompanied by other impurities and thus need to be purified using chromatographic techniques such as high performance liquid chromatography. By choosing an appropriate column and solvent system, Sermorelin can be isolated and other impurities removed.
It should be noted that the above description is a simplified overview of the synthesis of Sermorelin in general laboratories. Actual synthesis methods may vary depending on the research laboratory, manufacturer or patent protection. For specific laboratory synthesis methods and detailed chemical steps, it is recommended to refer to relevant scientific literature, patent documents or drug synthesis manuals, or consult with chemical experts with expertise in the field of peptide synthesis.
Sermorelin is a polypeptide hormone with some specific responsive properties. For these specific properties, a detailed description is given in the following text:
During the synthesis of Sermorelin, the amino acids are arranged in reverse order and linked together. This inverted arrangement is to ensure that the polypeptide chains fold correctly and form biologically active structures.
The α-hydrogen atoms in the amino acid residues of Sermorelin can participate in the nitrogen hydrogenation reaction. Hydronitrogenation is a commonly used selective reduction reaction, which can selectively reduce aldehyde, ketone, and enone functional groups under specific conditions without affecting other functional groups.
Since Sermorelin contains 29 amino acids, under suitable conditions, a cyclization reaction may occur between them. The cyclization reaction is to form a ring structure by reacting the terminal amino acid of the polypeptide chain with functional groups (such as carboxylic acid) on other amino acids.
The C-terminal end of Sermorelin is usually acylated to increase its stability and biological activity. This is usually carried out under basic conditions by using an appropriate acylating reagent such as an anhydride.
Sulfur-containing amino acid residues (such as cysteine) in Sermorelin powder may participate in oxidation reactions. These reactions can lead to the formation of disulfide bonds, thereby affecting the three-dimensional structure and biological activity of the polypeptide.
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