If you have been reading about ACTH(4-10) and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2026-02-11. Numbers and descriptions here follow the published literature rather than marketing material.
Published research has focused mainly on neurological and cognitive endpoints in animal models, with proposed mechanisms involving brain-derived neurotrophic factor and related signalling pathways. A substantial share of the human data originates from a limited number of research groups, and independent replication in other countries remains sparse. Regulatory status reflects that distribution: the peptide is registered as a medicine in Russia and appears in some neighbouring markets, while elsewhere it is handled as a research chemical without approved therapeutic labelling. Questions about dose-response relationships, long-term effects, and comparability across studies are still open.
Lyophilised powder is normally kept at -20 °C in a desiccated container, with some suppliers recommending -80 °C for long-term archival storage. Repeated freeze-thaw cycles are the most common cause of avoidable loss, so aliquoting before freezing reduces variability between working sessions. Dissolved peptide is far less stable than the dry solid and is usually prepared fresh or held briefly at 4 °C. Aqueous solutions support both hydrolysis of the backbone and oxidation of the N-terminal methionine, and these two routes dominate degradation under ordinary laboratory conditions.
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.
| Property | Value | Notes |
|---|---|---|
| Purity assay | RP-HPLC, UV 214 nm | Typical research grade 95 percent or higher |
| Mass confirmation | ESI-MS or MALDI-TOF | Compared with theoretical value |
| Main degradation route | Methionine oxidation | Sulfoxide formation in solution |
| Powder storage | -20 °C, desiccated | Amber vial, minimal headspace |
| Working solution | Sterile water or saline | Prepare fresh; avoid repeated thawing |
Verification of a supplied batch generally combines a certificate of analysis with independent testing, because certificates are self-reported documents. A typical package includes a chromatographic trace, a mass spectrum, and a stated water or counter-ion content. Batch-to-batch consistency matters more than a single purity figure when results are compared across experiments. No single mandatory standard governs research-grade peptide release, so laboratories are expected to define their own acceptance criteria. Residual trifluoroacetate from purification is a frequently overlooked counter-ion.
Lyophilized material is chemically stable for extended periods when kept dry, cold, and protected from light. The powder is hygroscopic, so vials should be warmed to room temperature before opening to reduce condensation on the contents. Once dissolved, the peptide is far less stable because peptide bonds are susceptible to hydrolysis and the methionine residue can oxidize. Solutions are typically aliquoted and held at 2-8 °C for short intervals or frozen for longer ones, and repeated freeze-thaw cycles should be avoided.
Routine characterization relies on reversed-phase high-performance liquid chromatography to establish purity and on mass spectrometry to confirm molecular identity. Electrospray ionization and matrix-assisted laser desorption ionization are both used for mass verification. Amino acid analysis and peptide mapping can detect sequence errors. Common impurities include truncated sequences, methionine sulfoxide formed by oxidation, and deamidated products. Chromatograms are usually recorded near 214 nm, where the peptide backbone absorbs, and purity is reported as the percentage area of the principal peak.
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.
Published research covers ischemic stroke, traumatic brain injury, cognitive impairment, optic nerve conditions and attention-related measures. Much of the human evidence comes from small trials conducted in one country, which limits how far the results generalize. Animal models supply the larger share of the data, and effects seen in rodents do not transfer automatically to people. Reviews have noted that methodological reporting is often incomplete, making it difficult to pool results or compare treatment schedules across studies.
Pharmacokinetic accounts emphasize rapid breakdown. After intravenous dosing the intact peptide disappears from blood within minutes, and nasal delivery produces low but measurable concentrations. Metabolites rather than the parent molecule may account for part of the observed activity, although the relative contribution is unresolved. Dosing in the literature varies widely and no optimal schedule has been agreed. These gaps are regularly cited as a reason the findings have not produced broad clinical adoption beyond the original research setting.
Proposed mechanisms center on neurotrophic signaling rather than on classical melanocortin receptor activation. Rodent experiments have reported shifts in the expression of brain-derived neurotrophic factor and nerve growth factor after administration, together with changes in the associated receptor systems. Several authors argue that the peptide acts largely through its degradation products and their interaction with peptidergic pathways, but this remains a hypothesis rather than a settled finding. No single molecular target has been identified in a way that the field broadly accepts.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Reversed-phase HPLC gives the main purity figure, most often with UV detection near 214 nanometres. Mass spectrometry then confirms the molecular mass. Together the two methods distinguish a correct sequence from a closely related impurity.
The main chemical risks are methionine oxidation and backbone hydrolysis in solution. Moisture and repeated temperature cycling accelerate both processes. Dry powder held cold and desiccated is considerably more stable than any reconstituted preparation.
It holds a medicine registration in Russia, where it has been used clinically for decades. In most other countries it is treated as a research chemical. That split explains the uneven distribution of clinical literature.
The sequence is Met-Glu-His-Phe-Pro-Gly-Pro, a seven-residue peptide. The first four residues correspond to the ACTH(4-10) fragment, and Pro-Gly-Pro is added at the C-terminus. N-acetylated versions also appear in the literature and differ in mass.