The short version of semax fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2025-10-28 and is reviewed periodically as new material appears.
Russian regulatory authorities approved the peptide for nasal administration, and it remains listed in the national pharmacopoeia under several trade names. Documented indications include acute ischemic stroke, transient ischemic attacks, traumatic brain injury, and certain ophthalmological and neurological conditions. Physicians also prescribe it for cognitive complaints in older patients, although the evidence base for that use is thinner. Outside Russia and a few neighboring states, the substance is not an approved medicine and is sold instead as a research chemical.
Later generations of the molecule include an N-acetylated form and an amidated form, both marketed online alongside the parent peptide. These variants differ in terminal chemistry and stability, and they are frequently discussed in the same breath even though they have not been compared in controlled trials. Supply outside formal healthcare systems comes largely from laboratories that synthesize peptides to order. Purity and identity of these materials vary widely, and no single body oversees the international trade.
Semax is a synthetic heptapeptide with the sequence Met-Glu-His-Phe-Pro-Gly-Pro. Its design combines the ACTH(4-7) core fragment with a C-terminal Pro-Gly-Pro extension, a modification intended to improve stability and prolong activity. The molecule is hydrophilic, carries no lipid chains or glycosylation, and has a theoretical mass just over 810 daltons in its free form. All seven residues are proteinogenic amino acids, so no non-natural building blocks appear in the backbone. A free N-terminal methionine and C-terminal proline define the unmodified parent peptide.
The compound was developed during the 1980s at the Institute of Molecular Genetics in Moscow as part of research on fragments of adrenocorticotropic hormone. Early work examined short ACTH-derived sequences that retained neurotrophic effects while lacking the endocrine activity of the full hormone. Semax entered clinical use in Russia during the 1990s, where it received registration for several neurological indications. Outside that region it remained primarily a laboratory research material rather than an approved therapeutic. English-language literature on it grew more slowly and frequently cited the original Russian studies.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic heptapeptide | Analog of an ACTH fragment |
| Amino acid length | Seven residues | Met-Glu-His-Phe-Pro-Gly-Pro |
| Origin | Moscow, 1980s | Institute of Molecular Genetics |
| Approved regions | Russia and some neighboring states | Not cleared in Western markets |
| Common trade names | Multiple national brands | Sold as a nasal formulation |
Semax is a synthetic peptide created in the Soviet Union during the early 1980s by researchers working in Moscow. It was built from the short adrenocorticotropic hormone fragment known as ACTH(4-10), and the chain was then extended with three additional amino acids. The resulting molecule was named semax and entered clinical use in Russia in 1994. It is generally described as a nootropic and neuroprotective agent rather than as a hormone analogue.
The parent fragment ACTH(4-10) carries the sequence Met-Glu-His-Phe-Arg-Trp-Gly. Semax replaces the arginine and tryptophan positions with a proline-glycine-proline tail, giving Met-Glu-His-Phe-Pro-Gly-Pro. That change removes residues associated with adrenal stimulation, so the peptide does not drive cortisol release the way full ACTH does. This distinction shapes how the compound is grouped in the literature, where it sits with neuropeptides and peptide neuromodulators rather than with corticosteroids.
Regulatory status varies sharply by country. Semax is registered for medical use in Russia, where it appears in formularies as a nasal solution, and it also holds registration in a small number of neighbouring states. It has no approval from the United States Food and Drug Administration or the European Medicines Agency, and it is not a scheduled controlled substance in most jurisdictions. Elsewhere it circulates mainly as laboratory material, so purity documentation comes from suppliers rather than from a national pharmacopoeia.
该化合物于二十世纪八十年代在俄罗斯被开发，相关工作由俄罗斯科学院分子遗传学研究所的研究团队主导。开发目标并非复制 ACTH 的完整激素活性，而是寻找保留其神经作用方向、同时去除促肾上腺皮质激素释放效应的短肽片段。研究记录显示，这一方向促成了多个相关短肽的合成与筛选，而 Semax 是其中被研究最广泛的一个。当地文献常以 Семакс 这一名称指代它。
研究兴趣主要集中在神经营养因子相关的路径上，包括脑源性神经营养因子与神经生长因子的表达变化。部分实验报告称在特定条件下观察到这些因子的水平上升，但具体信号通路和剂量依赖关系仍未完全厘清。多数公开数据来自细胞模型和动物实验，人体对照研究数量有限。因此，该化合物的作用机制在文献中属于活跃讨论，而非已经确立的定论。
Semax is a synthetic heptapeptide with the sequence Met-Glu-His-Phe-Pro-Gly-Pro. It corresponds to the ACTH(4-7) fragment extended at the C-terminus by a Pro-Gly-Pro tripeptide, an addition intended to slow enzymatic breakdown. The molecular formula is C37H51N9O10S and the molecular mass is approximately 814 daltons. In the literature it is often described as an ACTH(4-10) analog, although that label reflects a naming convention as much as a precise structural relationship. The compound was developed in Russia and remains most closely associated with that research tradition.
Laboratory descriptions of the material are consistent across suppliers. It appears as a white to off-white lyophilized powder that dissolves readily in water and in polar organic solvents such as dimethyl sulfoxide. Aqueous solutions are clear and colorless at low concentrations. Because the peptide contains methionine, oxidation at the sulfur atom is a recognized degradation pathway, and handling notes usually call for protected, desiccated storage. Reported purity for research-grade lots is generally above 95 percent as measured by reversed-phase high-performance liquid chromatography.
The compound is registered in Russia as a pharmaceutical product, most commonly formulated as a nasal solution, and has been used in that setting since the 1990s. Outside that jurisdiction it is generally handled as a research chemical rather than an approved medicine. Regulatory status therefore differs sharply between countries, and material sold internationally may not correspond to the Russian pharmaceutical formulation. Documentation with commercial samples is typically limited to a certificate of analysis covering purity and identity, not clinical status or local legal classification.
The Gunditjmara, a local Aboriginal Australian people in south-western Victoria, Australia, may have raised short-finned eels as early as about 4,580 BCE. Evidence indicates they developed about 100 km2 (39 sq mi) of volcanic floodplains in the vicinity of Lake Condah into a complex of channels and dams, and used woven traps to capture eels, and to preserve them to eat all year round. The local Budj Bim Cultural Landscape, a World Heritage Site, is one of the oldest known aquaculture sites in the world. Anthropologist Peter Sutton has disputed that these eel trapping systems qualify as aquaculture as there is no evidence they involved the breeding, feeding, protecting, or rearing of eels. Oral tradition in China tells of the culture of the common carp, Cyprinus carpio, as long ago as 2000–2100 BCE (around 4,000 years BP), but the earliest significant evidence lies in the literature, in the earliest monograph on fish culture called The Classic of Fish Culture, by Fan Li, written around 475 BCE (c. 2475 BP). Another ancient Chinese guide to aquaculture, wriiten by Yang Yu Jing around 460 BCE, shows that carp farming was becoming more sophisticated. The Jiahu site in China has circumstantial archeological evidence as possibly the oldest aquaculture locations, dating from 6200BCE (about 8,200 years BP), but this is speculative. When the waters subsided after river floods, some fish, mainly carp, were trapped in lakes. Early aquaculturists fed their brood using nymphs and silkworm faeces, and ate them.
During the first phase, from 1804 to 1806, it was a conservative reaction to new abuses by the Janissaries and Dahis, after they killed Hadji Mustafa Pasha (vizier of the Sanjak of Smederevo). He had created a militia of Serbs fighting the Janissaries that were expelled from Belgrade and had found refuge with Osman Pazvantoğlu, governor of the Sanjak of Vidin (in present-day Bulgaria), who pursued his own policy and sought independence, which brought him into conflict with the Serbs and later with the Sublime Porte. The Janissaries managed to return to Belgrade and realized the Slaughter of the Knezes. Thus, the Serbs appealed to Sultan Selim III for assistance against the Dahis, who had since rejected the authority of the Porte. Also, Karađorđe negotiated with the Austrian captain Sajtinski. At this meeting, he expressed the wish of the Serbian people that the Austrian Empire receive them as a kingdom under its protection like in the past, as occupation of 1788–1791 was still a fresh memory. However, the Austrian authorities, due to difficulties with Napoleon and because they wanted to maintain their neutrality in order to be correct with the Porte, could not accept his offers. So, the Serbs were forced to ask for the protection of the Russians, and therefore, on 3 May 1804, the Serb leaders sent a letter to the Russian envoy in Constantinople, in which they spoke of the problems and wishes of the Serbian people, but they also stressed that they would continue to be loyal to the Sultan.
In humans, evidence of a frameshift mutation in the bHLH domain of HAND1 has been correlated with hypoplastic left heart syndrome (a serious form of congenital heart disease where the left side of the heart is severely underdeveloped), aiding in the implication that HAND1 expression is a factor to patients with the disease. However, a lack of HAND1 in the distal regions of the Neural Crest has no effect on cranial feature formation. Mutation of HAND1 has been shown to hinder the effect of GATA4, another vital cardiac transcription factor, and is associated with congenital heart disease. The lack of HAND1 detection in the developing embryo leads to many of the structural defects that causes heart disease and facial deformities while the dosage of HAND1 relates to the severity of these maladies.
Sources: en.wikipedia.org
== Structure and enzymatic activity == FAP is a 760 amino acid long type II transmembrane glycoprotein. It contains a very short cytoplasmic N terminal part (6 amino acids), a transmembrane region (amino acids 7–26), and a large extracellular part with an alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain. A soluble form of FAP, which lacks the intracellular and transmembrane part, is present in blood plasma. FAP is a non-classical serine protease, which belongs to the S9B prolyl oligopeptidase subfamily. Other members of the S9B subfamily are DPPIV, DPP8 and DPP9. FAP is most closely related to DPPIV (approximately 50% of their amino acids are identical). The active site of FAP is localized in the extracellular part of the protein and contains a catalytic triad composed of Ser624 Asp702 His734 in humans and mice. FAP is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity. Several bioactive peptides and structural proteins were reported to be cleaved by FAP, such as neuropeptide Y (NPY), Peptide YY, Substance P (SP), and B-type natriuretic peptide (BNP), human fibroblast growth factor 21 (FGF-21), human alpha2 antiplasmin and denatured collagen I and III. NPY, FGF-21 and alpha2 antiplasmin are considered to be physiological FAP substrates.
== Discovery and structure elucidation == Kedarcidin was first discovered in 1992 when bioassays conducted at Bristol-Myers Squibb indicated the presence of a DNA-damaging chromoprotein in the fermentation broth of an Actinomycete strain. The involvement of a non-peptidic chromophore was deduced by UV spectroscopy, and reverse-phase chromatography was used to separate this noncovalently bound chromophore from its apoprotein host. This isolate—kedarcidin chromophore—decomposed readily under ambient conditions and was shown to possess cytotoxicity (IC50 0.4 ng/ml, HCT-116 human colorectal carcinoma cell line). Subsequent NMR, mass spectrometry, chemical degradation, and derivatization experiments enabled the isolation team to identify the key structural features of kedarcidin chromophore, including the enediyne bicyclic core, the ansa-bridging chloropyridyl ring, the mycarose and kedarosamine sugars, and the naphthoamide appendage. However, due to the challenges posed by the complex structure, the initial report had several errors. The bicyclic core proved particularly difficult to deconvolute, as the interpretation of NOE correlations led the researchers to misassign the relative stereochemistry of the core stereotetrad. Moreover, as global absolute chemistry was assigned on the basis of NOE correlations between the stereodefined L-mycarose sugar and the aglycone, the errors of the stereotetrad propagated to the other two stereocenters of the aglycone. Connectivity of the naphthoamide group to the ansa bridge was also misjudged in the initial report.
A degron can be converted into its active form by a post-translational modification such as phosphorylation of a tyrosine, serine or threonine residue. In this case, the ubiquitin ligase exclusively recognizes the phosphorylated version of the substrate due to stabilization within the binding site. For example, FBW7, the F-box substrate recognition unit of an SCFFBW7ubiquitin ligase, stabilizes a phosphorylated substrate by hydrogen binding its arginine residues to the phosphate, as shown in the figure to the right. In absence of the phosphate, residues of FBW7 repel the substrate.
Sources: en.wikipedia.org
== Causes == The mechanisms underlying metabolic syndrome are under investigation and only partially elucidated. Most affected people are older, obese, sedentary, and have some degree of insulin resistance. Stress can also contribute. Important risk factors include diet (particularly sugar-sweetened beverages), genetics, aging, sedentary behavior or low physical activity, disrupted chronobiology/sleep, mood disorders and some medications, and excessive alcohol use. The pathogenic role of excessive adipose expansion under sustained overeating and resulting lipotoxicity has also been proposed. Markers of systemic inflammation including C-reactive protein, fibrinogen, interleukin 6, and tumor necrosis factor-alpha (TNF-α) are often increased. Some research has focused on increased uric acid levels from dietary fructose. Modern "Western diet" patterns with high intake of energy-dense processed foods are a factor in the development of metabolic syndrome. Rather than total adiposity, the core clinical component is visceral/ectopic fat, and the principal metabolic abnormality is insulin resistance. A chronic energy surplus unmatched by activity may lead to mitochondrial dysfunction and insulin resistance.
==== Plants ==== Progesterone has been positively identified in the plant Juglans regia, a species of walnut. In addition, progesterone-like steroids are found in the plant Dioscorea mexicana, part of the yam family native to Mexico. Dioscorea mexicana contains a steroid called diosgenin which is taken from the plant and converted into progesterone. Diosgenin and progesterone are also found in other Dioscorea species, as well as in other plants that are not closely related, such as fenugreek. Another plant that contains substances readily convertible to progesterone is Dioscorea pseudojaponica, native to Taiwan. Research has shown that the Taiwanese yam contains saponins—steroids that can be converted to diosgenin and thence to progesterone. Many other Dioscorea species of the yam family contain steroidal substances from which progesterone can be produced. Among the more notable of these are Dioscorea villosa and Dioscorea polygonoides. One study showed that the Dioscorea villosa contains 3.5% diosgenin. Dioscorea polygonoides has been found to contain 2.64% diosgenin, as shown by gas chromatography-mass spectrometry. Many of the Dioscorea species that originate from the yam family grow in countries with tropical and subtropical climates.
=== SEC-TS === Size exclusion chromatography can be used directly to access protein stability in the presence or absence of ligands. Samples of purified protein are heated in a water bath or thermocycler, cooled, centrifuged to remove aggregated proteins, and run on an analytical HPLC. As the melting temperature is reached and protein precipitates or aggregates, peak height decreases and void peak height increases. This can be used to identify ligands and inhibitors, and optimize purification conditions. While of lower throughput than FSEC-TS, requiring large amounts of purified protein, SEC-TS avoids any influence of the fluorescent tag on apparent protein stability.
== Release == PYY is found in L cells in the mucosa of gastrointestinal tract, especially in ileum and colon. Also, a small amount of PYY, about 1-10%, is found in the esophagus, stomach, duodenum and jejunum. PYY concentration in the circulation increases postprandially (after food ingestion) and decreases by fasting. In addition, PYY is produced by a discrete population of neurons in the brainstem, specifically localized to the gigantocellular reticular nucleus of the medulla oblongata. C. R. Gustavsen et al. had found PYY-producing cells located in the islets of Langerhans in rats. They were observed either alone or co-localized with glucagon or PP. PYY is released by the L-cells of the gastrointestinal tract following food intake, and there are two main endogenous forms: PYY1-36 and PYY3-36. PYY1-36 is rapidly processed by the enzyme DPP4 to the 34-amino acid peptide PYY3-36. DPP4 hydrolyses PYY and removes the first two amino acids, tyrosine and proline, at the N-terminal, which changes the receptor selectivity. As a result of this, PYY3-36 has a high selectivity for the Y2-receptor, compared to PYY1-36 which has selectivity for the Y1, Y2, and Y5 receptors. It is thought that the Y1 receptor requires both the C-terminus and N-terminus for recognition, binding and then subsequent activation. The Y2 receptor is thought to have a smaller receptor site and also only requires the C-terminus for recognition. This could explain the reduced affinity for PYY3-36 on any other Y receptor other than Y2.
Sources: en.wikipedia.org
It originated at the Institute of Molecular Genetics in Moscow during the 1980s. The work was carried out by a Russian research group that specialized in peptide neuropharmacology.
It is registered as a medicine in Russia and has been used clinically there for decades. No regulatory agency in Western Europe or North America has approved it for any indication.
Semax corresponds to the four-to-ten fragment of adrenocorticotropic hormone. Because it omits the first three residues, it lacks the adrenal-stimulating action of the full hormone.
It is a synthetic seven-amino-acid peptide built from the ACTH(4-7) sequence plus a Pro-Gly-Pro tail. It belongs to the family of short ACTH fragments studied for nervous-system effects. Its backbone contains only standard amino acids.