ACTH(4-10) raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
This page was last updated on 2026-08-01 and is reviewed periodically as new material appears.
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.
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 |
|---|---|---|
| Chemical class | Synthetic heptapeptide | ACTH(4-7) analogue |
| Sequence | Met-Glu-His-Phe-Pro-Gly-Pro | Free N terminus, unmodified side chains |
| Molecular weight | 813.9 Da | Free base; salt forms differ |
| Appearance | White to off-white powder | Lyophilised solid |
| Solubility | Freely soluble in water | Hydrophilic; polar solvents preferred |
Reported pharmacological work centers on neurotrophic signaling, including changes in BDNF and NGF expression in hippocampal tissue in animal models. Human data come largely from studies conducted in Russia, and how well those results generalize to other populations remains an open question. Regulatory status differs sharply by jurisdiction: Semax is a registered prescription medicine in Russia, while it holds no approved marketing status in the United States or the European Union. Outside such jurisdictions it is generally handled as a research chemical, which affects both documentation and quality expectations.
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.
Claims about enhanced focus, memory, or mood in healthy people rest mostly on anecdotal reports and community discussion rather than on controlled data. It remains unclear whether any cognitive benefit observed in patients recovering from brain injury would extend to uninjured users. Dose-response relationships, long-term safety, and interactions with other drugs are not well characterized in the peer-reviewed literature. Questions about optimal route of administration and treatment duration likewise remain open.
Semax binds to melanocortin receptors and is thought to influence neuronal survival and plasticity rather than to act through the adrenal axis. Laboratory work has shown increased expression of brain-derived neurotrophic factor and nerve growth factor in treated tissue. Changes in c-Fos, a marker of neuronal activation, have also been reported. Because the peptide is rapidly degraded by peptidases, its effects are generally attributed to downstream signaling cascades rather than to sustained receptor occupancy.
=== Microfibrilated cellulose === Micro cellulose (MFC) is a type of nanocellulose that is more heterogeneous than cellulose nanofibers or nanocrystals as it contains a mixture of nano- and micro-scale particles. The term is sometimes misused to refer to cellulose nanofibers instead.
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Sources: en.wikipedia.org
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The δDs of hydroxyl-bearing minerals of the mantle were estimated at −80‰ ~ −40‰ via analysis of the isotopic composition for juvenile water. Hydrogen minerals generally have large isotope effects, and the isotopic composition often follows the pattern observed for precipitation.
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Sources: en.wikipedia.org
=== Linear motifs === Linear motifs are short disordered segments of proteins that mediate functional interactions with other proteins or other biomolecules (RNA, DNA, sugars etc.). Many roles of linear motifs are associated with cell regulation, for instance in control of cell shape, subcellular localisation of individual proteins and regulated protein turnover. Often, post-translational modifications such as phosphorylation tune the affinity (not rarely by several orders of magnitude) of individual linear motifs for specific interactions. Relatively rapid evolution and a relatively small number of structural restraints for establishing novel (low-affinity) interfaces make it particularly challenging to detect linear motifs but their widespread biological roles and the fact that many viruses mimick/hijack linear motifs to efficiently recode infected cells underlines the relevance of this research area.
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Sources: en.wikipedia.org
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.
It contains the 4-7 fragment of adrenocorticotropic hormone extended at the C terminus. That truncation removes the region associated with steroidogenic activity. The design intent was to keep neurotrophic properties while avoiding full hormonal effects.
No natural source of the intact heptapeptide is known. It is produced by solid-phase peptide synthesis. Some related ACTH fragments arise as hormone processing products, but the Pro-Gly-Pro extension is a designed addition rather than a natural sequence.
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.