ACTH(4-10) is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Updated 2026-08-01. Numbers and descriptions here follow the published literature rather than marketing material.
Development took place during the 1980s at institutes of the Russian Academy of Sciences, where peptide fragments of ACTH were screened for cognitive and neuroprotective effects. The compound received regulatory approval in Russia as a nasal preparation, marketed for conditions such as ischemic stroke, transient ischemic attacks, and optic nerve disorders. Registration in other countries has not followed. Most published clinical reports originate from a small number of Russian research groups, and independent replication outside that setting remains limited. The regulatory status therefore differs sharply between Russia and the rest of the world.
Laboratory work points toward modulation of neurotrophic signaling, particularly expression of brain-derived neurotrophic factor and nerve growth factor in hippocampal tissue. Studies also describe effects on monoamine turnover, inflammatory mediators, and oxidative markers. These observations come mainly from animal models and cultured cells, so the causal chain in humans is not firmly established. Whether the reported molecular changes translate into measurable clinical benefit is an open question. Reviews generally present the mechanism as plausible rather than demonstrated.
Clinical evidence consists largely of small trials with modest sample sizes, often without independent replication. Reported endpoints include cognitive scores, recovery after stroke, and visual function, but study designs vary widely and few trials meet contemporary reporting standards. Systematic reviewers have noted a high risk of bias in several of these reports. No large multicenter trial conducted outside Russia has been published. The compound is therefore best described as investigational in most jurisdictions, with its clinical role still unresolved.
Once dissolved, the peptide is considerably less stable than the solid. Aqueous solutions are usually prepared at neutral to slightly acidic pH, filtered, and divided into single-use aliquots before freezing. Repeated freeze-thaw cycles are a common cause of avoidable loss and are best prevented by never refreezing a thawed aliquot. Adsorption to plastic and glass surfaces can lower the measured concentration of dilute solutions, particularly below roughly 0.1 mg/mL. Buffer choice, salt content, and container material all influence how much peptide remains detectable after storage.
Identity and purity are established with standard peptide methods. Reversed-phase HPLC with ultraviolet detection near 214 nm resolves the parent peak from deletion and truncation byproducts, and reports typically quote a main-peak percentage. Mass spectrometry by electrospray or MALDI-TOF confirms the expected molecular mass, while amino acid analysis or peptide mapping can verify composition when the sequence itself is in question. A certificate of analysis that pairs a chromatogram with a mass spectrum is more informative than a purity figure alone. Counter-ion content and residual solvents are separate specifications and are frequently omitted.
Semax is normally supplied as a lyophilized powder, and that form is the most stable. Suppliers commonly recommend storage at -20 °C in a desiccated container protected from light, with short-term handling at room temperature limited to weighing and transfer. Powder that has absorbed moisture degrades faster, so vials should be warmed to ambient temperature before opening to prevent condensation on the contents. Hygroscopic behavior is typical of short hydrophilic peptides, and humidity control matters more than temperature alone for long-term retention.
| Property | Value | Notes |
|---|---|---|
| Sequence | Met-Glu-His-Phe-Pro-Gly-Pro | Heptapeptide; ACTH(4-10) analog extended at C-terminus |
| Molecular mass | ~813.9 Da | Free peptide, unmodified |
| Appearance | White to off-white powder | Typical lyophilized solid |
| Solubility | Soluble in water and saline | Also soluble in common aqueous buffers |
| Storage (solid) | -20 °C, desiccated | Protect from moisture and repeated thawing |
Regulatory status differs sharply between jurisdictions. In Russia the peptide is registered as a prescription nasal preparation, while agencies such as the United States Food and Drug Administration have not approved it for any indication. Products sold elsewhere are typically labeled for laboratory research only, and such labels shift responsibility for safe handling to the purchaser. Because the same name covers pharmaceutical-grade nasal drops and bulk research powder, identity and purity documentation becomes the main practical concern when comparing sources.
Semax is a synthetic seven-amino-acid peptide whose sequence extends the ACTH(4-10) fragment with a C-terminal proline-glycine-proline tripeptide. The commonly cited sequence is Met-Glu-His-Phe-Pro-Gly-Pro, giving a molecular formula near C37H51N9O10S and a molecular weight close to 813.9 g/mol. It belongs to the broader class of synthetic ACTH fragments studied for central nervous system effects rather than for adrenal steroid stimulation. In practice the material appears as a lyophilized white powder for laboratory work or as a dilute saline solution in clinical settings.
Development is attributed to researchers at the Institute of Molecular Genetics in Moscow during the early 1980s, building on earlier Soviet work with ACTH fragments. Russian regulatory approval followed for intranasal use, and the compound has remained commercially available there for decades. Most published human data originate from Russian and, later, some Eastern European clinical reports, which are not always accessible in English translation. Outside that region the material is generally handled as a research chemical rather than a licensed medicine.
溶液状态的稳定性明显低于冻干粉。肽类在水溶液中可能经历水解、氧化与聚集，其中甲硫氨酸和天冬酰胺等残基常是敏感位点。Semax 含有甲硫氨酸，因此氧化风险相对突出。工作液一般主张现配现用，或冷藏并在数日内用尽。缓冲液种类、pH 和离子强度都会影响降解速率，而关于最佳条件的公开数据并不统一。
常规纯度与身份确认依赖反相高效液相色谱，并辅以质谱测定分子量。氨基酸组成分析可用于验证序列构成，肽图分析则能进一步定位修饰或降解产物。杂质谱通常关注缺失序列肽、截短片段和氧化产物。不同方法的检出限并不相同，因此各实验室报告的纯度数值不宜直接横向比较。
Indian childhood cirrhosis is a form of neonatal cholestasis characterized by deposition of copper in the liver Alpha-1 antitrypsin deficiency is an autosomal co-dominant disorder of low levels of the enzyme alpha-1 antitrypsin Cardiac cirrhosis is due to chronic right-sided heart failure, which leads to liver congestion Galactosemia Glycogen storage disease type IV Cystic fibrosis Hepatotoxic drugs or toxins, such as acetaminophen (paracetamol), methotrexate, or amiodarone
In 1916, Grace acquired a controlling interest in the Pacific Mail Steamship Company. In 1921, Pacific received five 535 ft. President class ships from the United States Shipping Board for transpacific operation. In 1923, the US Shipping board decided to place the five ships up for bid and Dollar Shipping Company won the bid. With no large ships for the transpacific operations, Grace sold the Pacific Mail, its registered name, and goodwill to Dollar. Now without a transpacific service, Grace did not need the six intercoastal freighters and sold them to the American Hawaiian Line. At this time, Grace formed the Panama Mail Steamship Company, to operate the smaller ships that were formerly owned and used by the Pacific Mail in the Central American trade. These ships were not involved in the sale to Dollar. On the death of William R. Grace in 1904, he was succeeded by William L. Sauders as company president followed by Joseph Peter Grace Sr. (1872–1950) who became president in 1907. In 1938, the Colombian Line merged with Grace Line bringing an end to the Colombian Line. During World War II, Grace Lines operated transport for the U.S. War Shipping Administration, including the SS Sea Marlin. J. Peter Grace took over management of the company after his father suffered a stroke in 1945. After the war, the Grace line operated 23 ships totaling 188,000 gross tons, and 14 more on bareboat charters.
The secession of the Liberal Republican Union in March 1926, and the beginning of the Ditadura Nacional at the end of May of the same year, marked the end of the Nationalist Republican Party. In the early 1930s many former members of the PRN joined the National Union, ruling party of the Estado Novo.
=== Metal ion binding === Beyond the iron-sulfur proteins, many other metal cofactors in enzymes are bound to the thiolate substituent of cysteinyl residues. Examples include zinc in zinc fingers and alcohol dehydrogenase, copper in the blue copper proteins, iron in cytochrome P450, and nickel in the [NiFe]-hydrogenases. The thiol group also has a high affinity for heavy metals, so that proteins containing cysteine, such as metallothionein, will bind metals such as mercury, lead, and cadmium tightly. Silver ions can also bind tightly to cysteine and cause secondary structure changes in cysteine-containing peptides, e.g. leading to alpha helix formation. This is also the case for zinc fingers in which silver ions can replace zinc and form stable zinc/cysteine clusters with partial alpha helical structure. The extent of alpha helix formation increases with the number of cysteines.
Sources: en.wikipedia.org
=== Post-translational modifications === ECD-MS fragments can retain posttranslational modifications such as carboxylation, phosphorylation and O-glycosylation. ECD has the potential to do the top-down characterization of the major types of posttranslational modifications in proteins. It successfully cleaved 87 of 208 backbone bonds and provided the first direct characterization of a phosphoprotein, bovine β casein, simultaneously restricting the location of five phosphorylation sites. It has advantages over CAD to measure the degree of phosphorylation with a minimum number of losses of phosphates and for phosphopeptide/phosphoprotein mapping, which makes ECD a superior technique.
== Financials == The company has reported total income of Rs.2073.3345 crores during the Financial Year ended March 31, 2023 as compared to Rs.1181.7454 crores during the Financial Year ended March 31, 2022. The company has posted net profit of Rs.120.78 crores for the Financial Year ended March 31, 2023 as against net profit of Rs.49.6759 crores for the Financial Year ended March 31, 2022.
Also included are pouches of pickled vegetables (yellow radish, red cabbage, takana pickles, pickled hari-hari, or bamboo shoots) or salad (potato salad or tuna salad) and instant soup (miso, egg drop, wakame seaweed, or mushroom).
1915–1917 Experiments to find out the effects of food restriction on the life duration of rats, conducted by Thomas Osborne. Apparently, these were the first systematic experiments in this direction. These experiments remained little known. The method was popularized by Clive McCay in 1934–1935 (see further). 1910s–1930s Austrian physiologist Eugen Steinach was trying to achieve rejuvenation effects by means of different surgical operations such as partial vasectomy for men, ligation of fallopian tubes for women, transplantation of testicles, etc. And although later these operations were found to be ineffective, they allowed the researchers to recognize the role of the sexual glands and sexual hormones in the formation of the first and secondary sex characteristics, enriched physiology, laid the foundation for the science of sexology, formed the basis for sex reassignment surgeries. From 1921 to 1938, Eugen Steinach was nominated for the Nobel Prize many times (according to various sources, from 6 to 11 times), but never received it. 1910s–1930s Numerous experiments for obtaining rejuvenating effects by means of transplantation of organs and tissues. Among the most notable researchers who worked in this direction, there were Alexis Carrel (who developed the technology of anastomosis of blood vessels and advanced asepsis, a Nobel laureate of 1912), Mathieu Jaboulay, Emerich Ullmann, Jacques Loeb, John Northrop, Porfiry Bakhmetiev.
== Development == As with other antibody mimetics, the idea behind developing the Affibody molecule was to apply a combinatorial protein engineering approach on a small and robust protein scaffold. The aim was to generate new binders capable of specific binding to different target proteins with almost good affinity, while retaining the favorable folding and stability properties, and ease of bacterial expression of the parent molecule. The original Affibody protein scaffold was designed based on the Z domain (the immunoglobulin G binding domain) of protein A. These molecules are the newly developed class of scaffold proteins derived from the randomization of 13 amino acids located in two alpha helices involved in the binding activity of the parent protein domain. Lately, amino acids outside of the binding surface have been substituted in the scaffold to create a surface entirely different from the ancestral protein A domain. In contrast to antibodies, Affibody molecules are composed of alpha helices and lack disulfide bridges. The parent three-helix bundle structure is currently the fastest folding protein structure known. Specific Affibody molecules binding a desired target protein can be “fished out” from pools (libraries) containing billions of different variants, using phage display.
Sources: en.wikipedia.org
Semax is a synthetic seven-amino-acid peptide derived from a fragment of corticotropin. It is used in Russia as a nasal preparation, while elsewhere it is studied as a research compound. It is not approved as a medicine in most countries.
Its sequence corresponds to the 4-10 region of corticotropin extended by three residues. This fragment lacks the region responsible for adrenal steroid release, so it is explored for neural rather than hormonal effects. The relationship explains the compound's classification among ACTH-derived peptides.
It holds approval in Russia for several neurological indications as a nasal spray or drop formulation. Regulatory agencies in the United States and the European Union have not approved it. Products sold elsewhere are generally labeled for research use only.
Each freeze-thaw cycle can degrade a fraction of the peptide and promote aggregation. Dividing a stock solution into single-use volumes removes repeated cycling as a variable. It also limits the time a thawed solution spends at room temperature.