Kisspeptin(link:https://www.bloomtechz.com/synthetic-chemical/peptide/kisspeptin-powder-cas-1145998-81-7.html) is a small molecule peptide composed of 54 amino acid residues. Its molecular formula is C26H45N7O6S, with a molecular weight of 5477.73 Daltons. The amino acid sequence of kisspeptin peptide is highly conserved in different species, which means its basic structure remains unchanged in various organisms. Its precursor protein undergoes a series of modifications and splicing processes during the translation process, ultimately forming mature Kisspeptin. The structure consists of seven amino acid residues α- Helix, which is antiparallel to a structure composed of four amino acid residues β- Folding chain connection. This structure allows for binding to the G protein coupled receptor (GPR54) and activation of its signaling pathway.
Kisspeptin not only regulates female reproductive function in the central hypothalamus and pituitary gland, but also plays a role in the local ovaries. The local kisspeptin peptide in the ovary is not only involved in regulating the function of oocytes, granulosa cells, and corpus luteum, but also influenced by gonadotropins, photoperiod, sympathetic nervous system, and metabolism.
Kisspeptin is an important neuropeptide that regulates female reproductive function, expressed in the hypothalamus, pituitary, and ovaries, and has regulatory effects on various stages of HPOA. Kisspeptin is a product of the melanoma cell inhibitory gene KiSS-1, and is a natural peptide isolated by Kotani et al. in 2001 that exhibits agonistic activity against the orphan G protein coupled receptor GPR54 in human placenta.
Kisspeptin, also known as Kiss1 peptide or RFRP-1 peptide, is a neuropeptide found in the human body.
1. Chemical composition: Kisspeptin is a small molecule peptide composed of 54 amino acid residues, with a molecular formula of C26H45N7O6S and a molecular weight of 5477.73 Daltons. Its structure includes a hydrophilic N-terminal composed of nine amino acids and a hydrophobic C-terminal composed of four amino acids.
2. Chemical structure: The amino acid sequence of Kisspeptin is highly conserved in different species, which means its basic structure remains unchanged in various organisms. Its structure includes a relatively long N-terminal and a shorter C-terminal. In addition, Kisspeptin also has a cysteine (Cys) residue, which plays a crucial role in the disulfide process of peptides.
3. Secondary structure: The secondary structure of Kisspeptin is mainly composed of α- Composed of spiral and random curls. Among them, random curling occupies the majority of the peptide, while α- The helix only accounts for 20% of the total peptide. This secondary structure enables Kisspeptin to bind to the G protein coupled receptor (GPR54) and activate its signaling pathway.
4. Tertiary structure: The tertiary structure of Kisspeptin was determined by X-ray crystal diffraction and nuclear magnetic resonance (NMR) techniques. Its structure consists of seven amino acid residues α- Helix, which is antiparallel to a structure composed of four amino acid residues β- Folding chain connection. This structure enables Kisspeptin to bind to GPR54 and activate its signaling pathway.
5. Stereoscopic configuration: Kisspeptin is an S-configuration with a trans cycled stereoconfiguration. This three-dimensional configuration is crucial for the binding of Kisspeptin to GPR54 and the activation of its signaling pathway.
6. Modification and splicing: The Kisspeptin precursor undergoes a series of modifications and splicing processes during the translation process, ultimately forming a mature Kisspeptin. These processes include proline hydroxylation, glycine dehydrogenation, and disulfide bond formation. These modifications and splicing processes are crucial for the biological activity of Kisspeptin.
7. Stability: Kisspeptin has a certain degree of stability in the body. It has certain resistance to degrading enzymes such as acid, alkali, trypsin, and pepsin. However, under certain conditions, Kisspeptin may also be degraded, especially in high temperature, strong acid or alkali environments.
8. Chemical synthesis and recombination: Kisspeptin can be obtained through chemical synthesis or recombination methods. Chemical synthesis usually involves multiple tedious chemical reactions, including condensation, deprotection, desalination, and other steps. The recombination method, on the other hand, utilizes genetic engineering techniques to express the precursor protein of Kisspeptin in microorganisms such as Escherichia coli or yeast, and then undergoes post-processing to obtain mature Kisspeptin.
9. Detection and analysis: The content of Kisspeptin in organisms is very low, so sensitive analytical methods are needed to detect and analyze it. These methods include radioimmunoassay (RIA), enzyme-linked immunosorbent assay (ELISA), mass spectrometry (MS), etc. Among them, ELISA is one of the most commonly used detection methods, which can detect the content of Kisspeptin and its changes in the body.
Kisspeptin, also known as Kiss1 peptide or RFRP-1 peptide, is a neuropeptide first isolated from human placenta in 2001. It mainly participates in the regulation of the female reproductive system and stimulates the release of GnRH by binding to the G protein coupled receptor GPR54, thereby playing a role in the subsequent activities of the reproductive axis. In recent years, with in-depth research on Kisspeptin, it has been expressed in the central hypothalamus, pituitary, and ovary, regulating various links of HPOA, and may play an important role in diseases such as tumors. Therefore, the development prospects of Kisspeptin are worth looking forward to.
However, it should be pointed out that further research and clinical trials are needed to determine whether Kisspeptin can serve as a drug target for treating female reproductive system related diseases. In addition, more research support is needed to determine whether Kisspeptin has potential applications in treating other diseases such as tumors. In summary, Kisspeptin plays an important role as a neuropeptide in the regulation of the female reproductive system, and its development prospects are worth looking forward to. But more research and clinical trials are needed to verify its therapeutic potential. There are kisspeptins available for sale at the beginning of Shaanxi. If you need them, you can send an email for consultation.