Semax is a synthetic heptapeptide (Met-Glu-His-Phe-Pro-Gly-Pro) built from the ACTH(4-7) fragment of adrenocorticotropic hormone, extended with a C-terminal Pro-Gly-Pro tail for stability. Developed in the 1980s–90s at the Institute of Molecular Genetics of the Russian Academy of Sciences, it became one of Russia's established peptide pharmaceuticals — registered there for specific neurological indications — while remaining an investigational research compound elsewhere. Its research identity rests on a distinctive combination: melanocortin-family activity with neurotrophic signaling, and no meaningful corticosteroid (hormonal) effect at research exposure levels.
From ACTH to a non-hormonal fragment
Full-length ACTH is the pituitary hormone that drives cortisol release. But fragments of its sequence — particularly residues 4 through 10 — had been known since the mid-20th-century "neuropeptide" era to influence behavior and learning in animal models independently of any hormonal effect. The Russian research program, associated with the laboratory of Igor Ashmarin and colleagues at Moscow State University and the Institute of Molecular Genetics, engineered Semax from that active fragment: the ACTH(4-7) core provides the neuroactivity, and the Pro-Gly-Pro extension protects the peptide from rapid degradation. Critically, published characterization describes Semax as lacking corticosteroid activity at research doses — the endocrine effect of ACTH maps elsewhere in the molecule.
How Semax works in research models
- Neurotrophin expression: animal studies report Semax upregulating brain-derived neurotrophic factor (BDNF) and nerve growth factor (NGF) expression, with downstream TrkB-receptor signaling effects — the mechanistic center of its research profile.
- Melancortin-receptor research: as an MSH-family fragment, Semax has been examined for interactions with melanocortin receptors (MC4/MC5) expressed in the CNS, though its full receptor map remains a research question.
- Monoamine modulation: research describes effects on dopaminergic and serotonergic turnover in CNS models — examined in the context of attention and stress-response research questions.
- Ischemia models: the Russian stroke-research program studied Semax in ischemia/reperfusion models, reporting neuroprotection-related endpoints that supported its domestic registration.
Research timeline
Development ran through the 1980s–90s in Russia, culminating in domestic registration in the 1990s for indications including recovery support in neurological research contexts. It appears on the Russian pharmaceutical list and has a substantial Russian-language literature. International research interest has grown since the 2010s, focused on its BDNF-pathway effects and its status as a rare peptide with formal (if domestic) regulatory history. Outside Russia it is not an approved drug; material supplied here is laboratory research material only.
Key published findings
- Neurotrophin studies: published animal work describes BDNF/NGF upregulation following Semax exposure, with functional endpoints examined in learning and memory models.
- Ischemia research: studies in experimental stroke models reported neuroprotection-associated markers, forming the basis of its Russian clinical research program.
- Non-hormonal characterization: multiple studies confirmed the absence of significant ACTH-like corticosteroid effects at research exposures — the key safety-distinction finding for the fragment class.
- Attention and monoamines: Russian clinical and preclinical literature examined attention-related endpoints and monoamine-system effects in study populations and models.
Context among related compounds
Semax is the CNS/neuropeptide entry in this library, distinct from the metabolic, GH-axis, and repair categories. Its melanocortin heritage connects it distantly to KPV (another melanocortin fragment, studied for inflammatory rather than CNS pathways) — together they illustrate how one hormone family yielded fragments with sharply different research applications.
What researchers examine
Active research questions include BDNF-pathway dose-response mapping, melanocortin-receptor pharmacology in CNS models, monoamine-turnover effects, neuroprotection mechanisms in ischemia models, and peptide-stability engineering (the Pro-Gly-Pro tail as a model modification). Its domestic regulatory history also makes it a case study in peptide-drug development pathways.
Frequently asked research questions
What is Semax derived from?
The ACTH(4-7) fragment of adrenocorticotropic hormone, extended with a Pro-Gly-Pro tail for stability — engineered to retain neuroactivity without corticosteroid (hormonal) activity.
Is Semax an approved drug?
It is registered in Russia for certain indications and appears on the Russian pharmaceutical list. It is not approved in the US or EU. Material supplied by Prestige Peptides is laboratory research material only, not for human use.
Does Semax affect cortisol like ACTH does?
Published characterization describes no significant corticosteroid activity at research exposures — the hormonal effect of ACTH maps to other regions of the full-length molecule.
What is its main research mechanism?
Neurotrophin-pathway engagement: studies report upregulation of BDNF and NGF expression in CNS models, alongside monoamine-modulation effects.
How is it supplied and verified?
Lyophilized powder in sealed vials, identity and purity verified at ≥99% by independent third-party HPLC analysis.
Is Semax related to other melanocortin peptides?
Yes — it derives from the ACTH/MSH family. Different fragments of that family have sharply different research profiles: Semax (CNS/neurotrophin), KPV (inflammatory pathways, non-pigmenting), and the pigmentation-fragment class. Shared ancestry does not imply shared application.
How should the research material be stored?
Lyophilized vials: frozen at -20°C or below for long-term storage, protected from light and moisture. After reconstitution under sterile laboratory conditions, keep refrigerated at 2–8°C and use within the protocol's validated window.
How the evidence base reads
Semax has a substantial Russian-language literature — animal mechanism studies plus domestic clinical research underlying its Russian registration — and a smaller but growing international preclinical literature focused on BDNF pathways. It has not undergone Western regulatory development. Researchers should note the literature's geographic concentration when weighing it.
Laboratory handling and stability
For long-term research storage, keep lyophilized vials frozen at -20°C or below, protected from light and moisture; short-term handling at 2–8°C is standard. Reconstitution should be performed only under sterile laboratory conditions with the laboratory-grade solvent specified by the research protocol, and reconstituted material should be kept cold, protected from light, and used within the validated window of the protocol. Record vial lot numbers and retain the certificate of analysis with study records — traceability is a baseline requirement for reproducible work.
Related research in this library
Form, handling, and verification
Semax is supplied as a lyophilized (freeze-dried) powder in sealed vials, with identity and purity verified at ≥99% by independent third-party HPLC analysis. Lyophilized material should be stored in a cool, dry environment away from light and handled per standard laboratory protocol with appropriate protective equipment.
View Semax research material →
Research Use Only. All materials referenced are supplied strictly for qualified in-vitro laboratory research. Not for human or veterinary use, and not intended to diagnose, treat, cure, or prevent any disease. Nothing in this article constitutes medical advice, dosing guidance, or a recommendation for human use.
Technical Specifications
Structural identifiers verified against the NIH PubChem database.
| Property | Value |
|---|---|
| Common designation | Semax |
| Alternate names | ACTH (4-7), Pro-Gly-Pro- |
| Amino acid sequence | Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP) |
| Chain length | 7 residues |
| Molecular formula | C37H51N9O10S |
| Molecular weight | 813.9 g/mol |
| CAS number | 80714-61-0 |
| PubChem CID | 9811102 |
| Physical form | Lyophilized white powder, sealed vial |
| Purity specification | ≥99% by third-party HPLC |
| Analytical methods | RP-HPLC, mass spectrometry |
| Documentation | Certificate of Analysis issued per lot |
Source: National Center for Biotechnology Information, PubChem Compound Summary — CID 9811102. Supplied for qualified in-vitro laboratory research only; not for human consumption.