If you have been reading about Semax 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 2025-09-14. Numbers and descriptions here follow the published literature rather than marketing material.
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.
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 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.
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.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic heptapeptide | Analogue of the ACTH(4-10) fragment |
| Amino acid sequence | Met-Glu-His-Phe-Pro-Gly-Pro | Single-letter form MEHFPGP |
| Molecular formula | C37H51N9O10S | Free peptide, nominal mass near 814 Da |
| First registration | 1994, Russia | Nasal formulation for neurological indications |
| Typical purity grade | 95% or higher by HPLC | Research material; higher grades used as reference standards |
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.
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==== Interpretation of results ==== HOMA-IR < 2: normal insulin sensitivity HOMA-IR > 2: possible insulin resistance HOMA-IR > 2,5: probable insulin resistance HOMA-IR > 5: typical results for type 2 diabetes SPINA-GR 1,41–9,00 mol/s: normal insulin sensitivity SPINA-GR ≤ 1,40 mol/s: insulin resistance SPINA-GR < 1,35 mol/s: typical results for type 2 diabetes
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Sources: en.wikipedia.org
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Although both ribosome display and mRNA display are in vitro selection methods, mRNA display has some advantage over the ribosome display technology. mRNA display utilizes covalent mRNA-peptide complexes linked through puromycin; whereas, ribosome display utilizes stalled, noncovalent ribosome-mRNA-peptide complexes. For ribosome display, selection stringency is limited to keep ribosome-mRNA-peptide in a complex because of the noncovalent ribosome-mRNA-peptide complexes. This may cause difficulties in reducing background binding during the selection cycle. Also, the peptides under selection in a ribosome display system are attached to an enormous rRNA-protein complex, a ribosome, which has a molecular weight of more than 2,000,000 Da. There might be some unpredictable interaction between the selection target and the ribosome, and this may lead to a loss of potential binders during the selection cycle. In contrast, the puromycin DNA spacer linker used in mRNA display technology is much smaller comparing to a ribosome. This linker may have less chance to interact with an immobilized selection target. Thus, mRNA display technology is more likely to give less biased results.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Registered medical products are most often 0.1% nasal drops. Research suppliers ship lyophilized powder, usually in milligram quantities, which is dissolved before use. The active peptide is the same in both cases; presentation and excipients differ.
No. The peptide is synthetic, although it is modelled on a fragment of a naturally occurring hormone. ACTH(4-10) is generated when ACTH is cleaved, but the Pro-Gly-Pro extension is not a known endogenous sequence. It is therefore a designed analogue rather than a natural metabolite.
The label reflects reported effects on attention, memory and recovery after neurological injury in regional clinical reports. Those reports are mostly small and have not been widely replicated outside the region. The classification is descriptive and does not imply a single defined mechanism.
It is registered as a pharmaceutical product in Russia, where it is typically supplied as a nasal solution. In most other countries it is not an approved drug and is traded as a research chemical instead. Approval status depends entirely on the jurisdiction involved.