Everything below concerns ACTH(4-10). We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2026-06-20. Where a claim depends on a specific study, the study is described rather than over-claimed.
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. It was derived from the ACTH(4-10) fragment, a short segment of adrenocorticotropic hormone that lacks the hormonal activity associated with the full-length peptide. Researchers at the Institute of Molecular Genetics in Moscow developed the compound during the 1980s. It has been registered as a pharmaceutical product in Russia and several neighbouring countries, where it is supplied as a nasal solution, and it is also sold internationally as a research chemical.
The proposed mechanism centres on neurotrophic signalling rather than direct receptor activation. Semax is reported to increase expression of brain-derived neurotrophic factor and nerve growth factor in several brain regions, and to shift the balance between excitatory and inhibitory neurotransmitter systems. Interaction with melanocortin receptors has been suggested because of the parent ACTH fragment. Many of these findings come from rodent studies, and the extent to which they translate to human physiology remains an open question.
| 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 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.
Terminology around the compound varies by source. It appears in catalogues and papers as Semax, as the heptapeptide ACTH(4-7)-Pro-Gly-Pro, and under various alphanumeric laboratory codes used by individual suppliers. These names refer to the same sequence but may imply different salt forms, purity grades, or counter-ions. Peptide databases usually list the free base mass, while product descriptions sometimes report acetate or trifluoroacetate salts with a different formula weight. Because naming conventions for research peptides are not standardised across vendors, checking the declared sequence and measured mass is more reliable than relying on a trade name alone.
当时的短肽研究普遍关注能否穿越血脑屏障、在低剂量下产生中枢效应，Semax 属于这一路线。鼻内给药是其主要使用方式，俄语文献报道的适应症涵盖缺血性卒中、短暂性脑缺血发作、认知功能减退以及视神经病变。这些研究大多发表在当地期刊上，样本规模与终点设置同西方试验惯例存在差异，国际同行对其临床证据的强度看法不一。
各国监管态度分化明显。俄罗斯按处方药管理，部分东欧国家留有使用记录；欧盟与美国未批准其作为药物上市，市面流通品通常标注为研究用化学品。身份差异意味着标示含量、纯度与无菌性缺少统一核查。体育领域还牵涉反兴奋剂名录，跨境携带则受目的地药品法规约束。
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.
Decreased TOR activity has been found to increase life span in S. cerevisiae, C. elegans, and D. melanogaster. The mTOR inhibitor rapamycin has been confirmed to increase lifespan in mice. It is hypothesized that some dietary regimes, like caloric restriction and methionine restriction, cause lifespan extension by decreasing mTOR activity. Some studies have suggested that mTOR signaling may increase during aging, at least in specific tissues like adipose tissue, and rapamycin may act in part by blocking this increase. An alternative theory is mTOR signaling is an example of antagonistic pleiotropy, and while high mTOR signaling is good during early life, it is maintained at an inappropriately high level in old age. Calorie restriction and methionine restriction may act in part by limiting levels of essential amino acids including leucine and methionine, which are potent activators of mTOR. The administration of leucine into the rat brain has been shown to decrease food intake and body weight via activation of the mTOR pathway in the hypothalamus. According to the free radical theory of aging, reactive oxygen species cause damage to mitochondrial proteins and decrease ATP production. Subsequently, via ATP sensitive AMPK, the mTOR pathway is inhibited and ATP-consuming protein synthesis is downregulated, since mTORC1 initiates a phosphorylation cascade activating the ribosome. Hence, the proportion of damaged proteins is enhanced. Moreover, disruption of mTORC1 directly inhibits mitochondrial respiration.
=== EC 1.99.2 Oxygenases (now covered by EC 1.13) === EC 1.99.2.1: deleted, now EC 1.13.11.12, lipoxygenase EC 1.99.2.2: deleted, now EC 1.13.11.1, catechol 1,2-dioxygenase EC 1.99.2.3: deleted, now EC 1.13.11.3, protocatechuate 3,4-dioxygenase EC 1.99.2.4: deleted, now EC 1.13.11.4, gentisate 1,2-dioxygenase EC 1.99.2.5: deleted, now EC 1.13.11.5, homogentisate 1,2-dioxygenase EC 1.99.2.6: deleted, now EC 1.13.99.1, inositol oxygenase
Circulatory system: pumping and channeling blood to and from the body and lungs with heart, blood, blood vessels Digestive system: digestion and processing food with salivary glands, esophagus, stomach, liver, gallbladder, pancreas, intestines, rectum, anus Endocrine system: communication within the body using hormones made by endocrine glands such as the hypothalamus, pituitary gland, pineal gland, thyroid, parathyroid glands, adrenal glands Immune system: the system that fights off disease; composed of leukocytes, tonsils, adenoids, thymus, spleen Integumentary system: skin, hair, nails Lymphatic system: structures involved in the transfer of lymph between tissues and the blood stream, the lymph and the nodes and vessels that transport it Musculoskeletal system: muscles provide movement and a skeleton provides structural support and protection with bones, cartilage, ligaments, tendons Nervous system: collecting, transferring and processing information with brain, spinal cord, nerves Reproductive system: the sex organs; in the female; ovaries, fallopian tubes, uterus, vagina, mammary glands, and in the male; testicles, vas deferens, seminal vesicles, prostate, penis Respiratory system: the organs used for breathing, the pharynx, larynx, trachea, bronchi, lungs, diaphragm Urinary system: kidneys, ureters, bladder, urethra involved in fluid balance, electrolyte balance, and excretion of urine
Sources: en.wikipedia.org
Elevated levels of bile acid and inflammatory proteins linked to GERD and microaspiration suggest that these factors may lead to the development of bronchiolitis obliterans in lung transplant recipients.
=== Medical === Odontostomatology: gingivitis, stomatitis, glossitis, aphthous ulcers, dental surgery and oral ulceration due to radiation therapy. Otorhinolaryngology: glandular fever, pharyngitis, tonsillitis, post-tonsillectomy, radiation or intubation mucositis. It may be used alone or as an adjunct to other therapy giving the possibility of increased therapeutic effect with little risk of interaction. In some markets, the drug is supplied as an over-the-counter cream (Lonol in Mexico from Boehringer Ingelheim) used for topical treatment of musculoskeletal system disorders: sprains, strains, bursitis, tendinitis, synovitis, myalgia, periarthritis.
==== Breast crawl ==== According to studies cited by UNICEF, babies naturally follow a process that leads to a first breastfeed. Shortly after birth, the infant relaxes and makes small movements of the arms, shoulders, and head. If placed on the mother's abdomen, the baby gradually inches towards the breast, known as the breast crawl and begins to feed. After feeding, it is normal for a baby to remain latched to the breast while resting. This is sometimes mistaken for a lack of appetite. Without interruptions, all babies follow this process. Rushing, by picking up and moving the infant to the breast, or interrupting the process, such as removing the baby to be weighed, may complicate subsequent feeding. Activities such as weighing, measuring, bathing, needle-sticks, and eye prophylaxis wait until after the first feeding.
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.
Semax is based on the ACTH(4-10) fragment, a seven-amino-acid segment of adrenocorticotropic hormone. The synthetic peptide retains the core sequence while removing regions associated with endocrine activity. This modification is intended to isolate effects on the nervous system.