���发背景与监管地位 — Reference Sheet

By Editorial Desk · published 2026-03-21 · last reviewed 2026-04-14 · Guide

A practical reference on Semax: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.

Reviewed 2026-04-14. Anything still debated is marked as such rather than presented as settled.

研发背景与监管地位

Semax 是人工设计的七肽，序列为 Met-Glu-His-Phe-Pro-Gly-Pro，骨架取自促肾上腺皮质激素片段 ACTH(4-10)。它于二十世纪八十年代在苏联的分子遗传学研究机构内合成。设计目标是保留该片段与注意力和记忆相关的活性，同时剔除促皮质激素释放等内分泌作用。此后俄罗斯将其登记为药品并进入临床使用。

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。

Semax Peptide Background and Identity

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.

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 at a glance

Chemical Identity and Research Background

Semax is a synthetic heptapeptide whose sequence is Met-Glu-His-Phe-Pro-Gly-Pro. The first four residues correspond to the ACTH(4-10) fragment, while the terminal Pro-Gly-Pro extension was added to improve metabolic stability. Its molecular formula is C37H51N9O10S and its monoisotopic mass is approximately 813.9 Da. The compound is classified as a peptide research chemical and as a registered pharmaceutical product in Russia, but it does not hold marketing approval in the European Union or the United States. Naming conventions vary across supplier catalogs.

Development of the compound took place in the Soviet Union during the 1980s, largely through peptide research groups affiliated with the Shemyakin-Ovchinnikov Institute and Moscow State University. Investigators screened fragments of adrenocorticotropic hormone for activity on the central nervous system while attempting to separate cognitive effects from hormonal ones. The shortened sequence was selected because it retained behavioral activity in animal models without stimulating corticosteroid release. Early publications described the molecule as an ACTH(4-10) analog.

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Background and Development

Semax is a synthetic heptapeptide developed in the Soviet Union during the 1980s by researchers at the Institute of Molecular Genetics in Moscow. It was designed as a truncated analog of adrenocorticotropic hormone, retaining only the fragment spanning residues four through ten. Investigators sought a peptide that would preserve the cognitive effects associated with ACTH while eliminating the hormonal stimulation of the adrenal cortex. The compound entered clinical use in Russia during the following decade.

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.

Semax Background and Molecular Structure

Semax is a synthetic heptapeptide whose sequence is Met-Glu-His-Phe-Pro-Gly-Pro. It was developed as a fragment analog of adrenocorticotropic hormone, modeled specifically on the ACTH(4-10) region. The first four residues reproduce that fragment, while a Pro-Gly-Pro tripeptide is appended at the C-terminus. Work on the compound originated in Russia, where it entered clinical use as an intranasal preparation. Its sequence places it among short regulatory peptides studied for effects on the central nervous system rather than on the adrenal axis.

The C-terminal Pro-Gly-Pro extension is not incidental. Proline-rich tails are known to resist several common peptidases, and the published literature attributes the longer half-life of Semax, relative to unmodified ACTH fragments, to this feature. The modification also removes the melanocyte-stimulating and corticosteroidogenic activity that characterizes longer ACTH-derived sequences. Because the molecule is small and hydrophilic, it is typically formulated as an aqueous solution for intranasal or parenteral delivery. Acetylation or amidation at the termini appears in closely related research peptides and shifts the mass by a fixed increment.

Semax Peptide Structure and Origin

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.

Background from the literature

== Catalysis == The sortase B enzyme catalyzes a cell wall sorting reaction with a surface protein where a signal NXTN motif is cleaved. In the result, the C-end of the protein is covalently attached to a pentaglycine cross-bridge through an amide linkage, thus tethering the C-terminus of protein A to the cell wall. It cleaves the protein precursor molecule at the NPQTN motif. The peptide bond between T and N of the NPQTN sorting motif is cleaved to form a tetrahedral acyl intermediate. The amino groups of the pentaglycine cross-bridges linked to the lipid II peptidoglycan precursor molecules are thought to function as nucleophile resolving acyl intermediates and creating an amide bond between the surface protein and lipid II with subsequent incorporation of this intermediate into the cell wall envelope. IsdC remains buried within the cell wall, not surface located like IsdA and IsdB anchored by Sortase A. This whole system work together to scavenge iron from haemoglobin.

Helene Langevin is an American medical scientist who served as the Director of the National Center for Complementary and Integrative Health (NCCIH) at the National Institutes of Health (NIH) between November 2018 and November 2025. She was a professor in the University of Vermont College of Medicine's Department of Neurological Sciences. She is best known for characterizing certain cellular and mechanical effects of acupuncture. She was also a Professor in Residence of Medicine at Harvard Medical School, Brigham and Women's Hospital. Prior to working at NIH, Langevin was the Director of the Osher Center for Integrative Medicine, jointly owned by Brigham and Women's Hospital and Harvard Medical School. Langevin was the principal investigator of studies funded by the National Institutes of Health. The Boston Globe describes her as a "celebrity" in the world of acupuncture.

== Application == As different proteins have different compositions of amino acids, different protein molecules precipitate at different concentrations of salt solution. Unwanted proteins can be removed from a protein solution mixture by salting out as long as the solubility of the protein in various concentrations of salt solution is known. After removing the precipitate by filtration or centrifugation, the desired protein can be precipitated by altering the salt concentration to the level at which the desired protein becomes insoluble. One demerit of salting out in purification of proteins is that, in addition to precipitating a specific protein of interest, contaminants are also precipitated as well. Thus to obtain a purer protein of interest, additional purification methods such as ion exchange chromatography may be required.

Sources: en.wikipedia.org

Reference notes

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Day of Defeat was followed by Day of Defeat: Source, a remake of the game that runs on Valve's Source engine. The Source remake included significant changes to Day of Defeat's gameplay, new maps, updated graphics, and improved physics. Released on September 26, 2005 to favorable reviews, the game was praised for its gameplay, audio, and graphics. Post-release, the game was supported by Valve with a number of subsequent updates, including versions of the game for OS X and Linux released in 2010 and 2013 respectively.

Sources: en.wikipedia.org

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