Semax — identity, handling and published literature

Semax is a synthetic heptapeptide of the melanocortin family, supplied as a lyophilised solid for laboratory use and described in the literature as an analogue of the adrenocorticotropic hormone fragment ACTH(4-10).

Presentation and physical properties

Semax is the sequence Met-Glu-His-Phe-Pro-Gly-Pro (one-letter: MEHFPGP). Its first four residues correspond to ACTH(4-7); the Arg-Trp-Gly portion of ACTH(4-10) is replaced by the tripeptide Pro-Gly-Pro. This substitution is why the molecule contains neither tryptophan nor tyrosine, which has direct consequences for how it is detected analytically, and why the literature refers to it interchangeably as an ACTH(4-10) analogue and as ACTH(4-7)PGP.

Reconstitution arithmetic

Reconstitution is a division. The mass stated on the vial is fixed; the concentration that results is that mass divided by the volume of diluent added. Nothing below is a recommendation about how much material to use in any experiment — it is the arithmetic relating a labelled mass to a withdrawn volume, and no more than that.

The relationship is:

concentration (mg/mL) = vial mass (mg) ÷ diluent volume (mL)

and, for a withdrawn volume:

mass withdrawn (mg) = concentration (mg/mL) × volume withdrawn (mL)

Worked for a 10 mg vial, the presentation NovoVita lists:

Molar figures use the average molecular weight of 813.9 g/mol. Two points of arithmetic hygiene apply. First, the displaced volume of the solid is not accounted for in the table: 10 mg of peptide occupies a small but non-zero volume, so a vial reconstituted with 1 mL of diluent holds marginally more than 1 mL of solution and the true concentration is marginally below 10 mg/mL. For most laboratory purposes this is within the error of the fill tolerance; where it is not, the solution should be prepared gravimetrically or made up to a mark. Second, the labelled mass is nominal peptide mass as sold, and if the certificate reports a net peptide content below 100 per cent then the mass of peptide actually present is lower than the label by that proportion, and every figure in the table scales with it.

Storage and stability

The lyophilised solid and the reconstituted solution are two different stability problems and should not be conflated.

Lyophilised. Dry, cold, dark and sealed is the stable state. The cake has little mobile water, which suppresses both hydrolysis and the oxidative chemistry described below. Vials held at −20 °C are the usual laboratory arrangement; lower temperatures do no harm. The failure modes for the dry solid are moisture ingress through a compromised stopper, repeated warming and cooling of the vial, and prolonged exposure to light.

In solution. Once water is present the molecule is on a clock. Aqueous solutions are conventionally aliquotted immediately and frozen, so that the working stock is thawed once rather than repeatedly. Short-term refrigerated storage of a working solution is common practice; the interval over which a given preparation remains within specification is a property of that preparation and its buffer, and can only be established by re-assaying it.

Freeze-thaw. Repeated cycling is more damaging than the number of cycles suggests, for reasons that are about the buffer rather than the peptide. As ice forms, solutes concentrate in the shrinking liquid fraction, and in sodium phosphate buffers the disodium salt crystallises preferentially, dropping the pH of the residual liquid by two units or more. The peptide therefore experiences a transient acid excursion at every freeze, invisible to any measurement made on the thawed solution. Single-use aliquots remove the problem rather than managing it.

Degradation routes specific to this sequence. Four of the seven residues carry distinct liabilities, and they are not equally important.

• Methionine at position 1 is the dominant route. The thioether side chain oxidises readily to the sulfoxide (a mass increase of 15.995 Da) and, under more forcing conditions, to the sulfone (+31.990 Da). Dissolved oxygen, headspace air, trace transition metals, peroxide contamination in polysorbate-containing buffers and ambient light all accelerate it. Because Semax has only one methionine, the sulfoxide is a single well-defined species and is straightforward to identify by mass spectrometry — it is the first impurity to look for in any aged solution.
• Histidine at position 3 is the second oxidative target, susceptible to metal-catalysed oxidation of the imidazole ring. The imidazole also chelates trace metals, which concentrates the catalyst on the molecule that is about to be damaged by it. Chelating agents in the buffer address this; adventitious metal from glassware or from the diluent is the usual source.
• The glutamate side chain at position 2 can undergo slow acid-catalysed isomerisation and imide-mediated rearrangement. This chemistry is far slower for glutamate than the corresponding aspartate pathway, which forms a five-membered succinimide; glutamate must form a strained six-membered glutarimide, so at neutral pH it is a minor route rather than a governing one.
• The backbone. Amide bond hydrolysis is the general route at pH extremes. The C-terminal Pro-Gly-Pro extension is the reason the molecule was constructed this way: bonds on the N-terminal side of proline resist most aminopeptidases, and that resistance is the stated design rationale for the tripeptide tail in the literature that describes the analogue.

Adsorptive loss to container surfaces, a serious problem for hydrophobic peptides at low concentration, is comparatively mild here — a computed XLogP of −2.8 and a polar surface area above 300 Ų describe a molecule with little affinity for polypropylene or borosilicate. It is not zero, and at sub-micromolar working concentrations it remains worth controlling.

Analytical identity

Reversed-phase HPLC. The standard configuration is a C18 stationary phase with a water/acetonitrile gradient and 0.1 per cent trifluoroacetic acid as ion-pairing modifier. Semax is very polar and elutes early; a shallow gradient starting at low organic content is needed to retain it and to resolve it from the more polar oxidation products, which elute earlier still.

Detection wavelength is the trap. Semax contains no tryptophan and no tyrosine, because the Pro-Gly-Pro extension replaced the Arg-Trp-Gly portion of ACTH(4-10). It therefore has no strong absorbance at 280 nm, and a purity or content figure generated at that wavelength is close to meaningless for this molecule. Detection belongs at 214–220 nm, where the amide bond itself absorbs. Phenylalanine contributes weak fine structure near 257 nm and histidine absorbs only in the far ultraviolet; neither supports quantification.

Mass spectrometry. Electrospray ionisation gives the expected series:

Tandem mass spectrometry confirms the sequence through the b and y ion series. Two features of this peptide shape the spectrum: the two prolines promote preferential cleavage of the amide bond on their N-terminal side, giving intense y ions at those positions, and the basic histidine influences where the mobile proton sits and therefore the relative intensities across the series. A published forensic method for detecting cognitive-enhancement research peptides in seized preparations used exactly this approach, developing a combined LC-MS/MS screen covering ten such peptides including Semax [24].

What area-percent purity does and does not measure. An HPLC purity figure expressed as area percent states one thing: the proportion of the total ultraviolet absorbance in a chromatogram that eluted under the main peak, at one wavelength, on one column, under one gradient. It is a useful number and it is routinely over-read. It does not establish:

• Identity. Area percent says a single species dominates; it does not say which species. Identity requires mass spectrometry, and sequence confirmation requires tandem mass spectrometry or amino acid analysis.
• Peptide content. A solid that is 98 per cent pure by HPLC may be substantially less than 98 per cent peptide by mass, because the remainder is counterion (trifluoroacetate or acetate) and residual water, neither of which appears in the chromatogram. Net peptide content is a separate determination — amino acid analysis or nitrogen determination — and the gap between the two figures is commonly in the range of a fifth to a third of the total mass.
• Co-eluting impurities. Deletion and truncation sequences differing by one residue can co-elute with the parent under a shallow gradient and be counted as main peak. Orthogonal separation, or mass spectrometric detection across the peak, is what resolves this.
• Anything without a chromophore at the detection wavelength. Inorganic salts, many residual synthesis solvents and non-absorbing process residues are invisible.
• Endotoxin, bioburden or elemental impurities. All are separate specifications with separate methods.

What the published literature investigated

What follows describes what published studies examined and what those studies reported. Every statement is a statement about a study, not about the molecule. The great majority of this body of work originates from a small number of collaborating institutes in Moscow; that observation is set out in the section on evidence gaps, because it bears on how the results should be weighed.

In vitro

Safarova and colleagues (2003) exposed cultured rat pheochromocytoma (PC12) cells to hydrogen peroxide and assessed cell survival by fluorescent staining, reporting a concentration-dependent reduction in the proportion of cells showing necrotic morphology, with the magnitude depending on when the peptide was added relative to the oxidative insult [1].

Grivennikov and colleagues (2008), working with primary rat basal forebrain cultures, reported an approximately 1.5- to 1.7-fold increase in the survival of cholinergic neurons and, at 100 nM, an increase in choline acetyltransferase activity. The same report noted no measured effect on GABAergic neurons or on glial proliferation. The authors stated explicitly that the implications of these observations for Alzheimer’s disease remained to be clarified [2].

Novosadova and colleagues (2019) established a screening system using human induced pluripotent stem cells and their neuronal derivatives, challenged with hydrogen peroxide, and compared several compound classes. In that assay Semax produced a protective effect of approximately 40 per cent, which the authors reported as lower than the roughly 70 per cent recorded for the endocannabinoid comparator N-docosahexaenoyl dopamine [3].

Rodent

A sustained line of work has examined neurotrophin gene and protein expression. Dolotov and colleagues (2003) reported stimulation of BDNF expression across several rat brain regions in vivo [4]. The same group (2006) reported that a single administration at 50 µg/kg was followed by a maximal 1.4-fold rise in hippocampal BDNF protein, a 1.6-fold rise in trkB tyrosine phosphorylation, and three-fold and two-fold increases in exon III BDNF and trkB mRNA respectively, alongside a change in conditioned avoidance responding [5]. Shadrina and colleagues (2010) mapped the time course of NGF and BDNF transcripts across hippocampus, frontal cortex and retina, reporting an initial decrease at 20 minutes followed by a rise that peaked around eight hours [6].

A second line concerns experimental cerebral ischaemia. Romanova and colleagues (2006) reported neuroprotective and antiamnesic effects in a model of ischaemic infarction of the cerebral cortex [7]. Stavchansky and colleagues (2011) described, in a study the authors themselves labelled a pilot, effects of Semax and of its C-terminal PGP fragment on brain cell morphology and proliferative activity during experimental ischaemia [8].

Transcriptomic work has attempted to identify what changes. Medvedeva and colleagues (2014) performed genome-wide analysis after middle cerebral artery occlusion in rats and reported that the expression changes were predominantly in immune system genes, together with altered expression of 24 vascular genes at three hours [9]; the same group (2017) reported in more detail on immune response gene regulation during ischaemic brain injury [10]. Filippenkov and colleagues (2020) reported transcriptome-level findings following ischaemia-reperfusion [11], and Sudarkina and colleagues (2021) added protein-level measurements in the same model, reporting upregulation of active CREB in subcortical structures and downregulation of MMP-9 and c-Fos in adjacent frontoparietal cortex at 24 hours [12].

Glazova and colleagues (2021) reported that Semax administration attenuated behavioural and neurochemical alterations in rat pups following early-life exposure to the SSRI fluvoxamine, including measures of anxiety-like behaviour, learning and brain biogenic amine levels [13].

One recent study is notable for originating outside the Russian research network. Liu and colleagues (2025), publishing in the British Journal of Pharmacology, examined a mouse spinal cord injury model and reported effects on functional recovery and on pyroptosis-related pathways, identifying the µ-opioid receptor gene Oprm1 as a molecular target and describing a deubiquitination mechanism [14].

Human

The human literature is small, old in its centre of gravity, and overwhelmingly Russian-language. It should be read with the limitations in the next section held in view throughout.

Gusev and colleagues (1997) published a clinical and electrophysiological study in acute hemispheric ischaemic stroke comprising 30 patients receiving the peptide alongside intensive therapy and 80 controls, reporting an influence on the rate of restoration of neurological function, particularly motor recovery [15]. Two ophthalmological reports followed: Polunin and colleagues (2000) compared three groups of patients with optic nerve disease and reported a favourable effect on the intensity and rate of recovery [16], and Kurysheva and colleagues (2001) reported on glaucomatous optic neuropathy in patients whose ophthalmic tone had been normalised [17]. Ivanikov and colleagues (2002) published a short report on peptic ulcer in which intranasal administration alongside standard medication was associated with higher healing rates than in controls [18].

Gusev and colleagues (2005) reported a study of 187 patients with cerebrovascular insufficiency, describing clinical improvement and reduced incidence of stroke and transient ischaemic attacks over the observation period [19]. This is the largest human study identified in the indexed literature. Serdiuk and colleagues (2007) published the only record in PubMed carrying the publication type “Randomized Controlled Trial”, a study of chronic partial denervation and quality of life in motor neuron disease [20].

Gusev and colleagues (2018) reported on 110 patients at different stages of ischaemic stroke, divided into early and late rehabilitation groups, with plasma BDNF, motor performance and disability scales as outcomes [21].

Two imaging studies in healthy volunteers examined resting-state brain networks rather than clinical endpoints. Lebedeva and colleagues (2018) studied 24 healthy volunteers (mean age 43.9 years) with resting-state functional MRI before and 5–20 minutes after intranasal administration or placebo, reporting a greater volume of the rostral, medial frontal subcomponent of the default mode network in the Semax group [22]. Panikratova and colleagues (2020) applied a whole-brain functional connectivity analysis in 52 healthy participants comparing Semax and Selank, reporting differences in connectivity between the right amygdala and temporal regions [23].

Evidence gaps and limitations

This is the section that matters most, and it is not softened.

There is no registered clinical trial. A search of ClinicalTrials.gov in August 2026, both as an intervention query and as a general term query, returned zero records for Semax. Not zero completed trials — zero records of any status, including planned, recruiting, terminated and withdrawn. Whatever human work exists was conducted outside the international trial registration system.

One record in the entire PubMed index carries the publication type “Randomized Controlled Trial” [20], and it is a Russian-language study in motor neuron disease, not in any of the areas where the compound is most often discussed. The stroke literature, which is the largest human body of work, is not indexed as randomised controlled trial evidence.

Nothing has been independently replicated outside Russia. The human studies are almost entirely from Russian institutions, published in Russian-language journals — Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova and Vestnik oftalmologii — with English abstracts but without the full methods, protocols or participant-level reporting that would allow external appraisal. Where the abstract is all that is available in English, the reader cannot assess randomisation, allocation concealment, blinding, outcome definition or handling of missing data. None of the reported clinical findings has been reproduced by an independent group in a different country.

The research network is narrow. Of the studies cited in this entry, N. F. Myasoedov appears as an author on the substantial majority, spanning the in vitro, rodent and human work and spanning nearly three decades. This is not an allegation of impropriety; it is a structural fact about the evidence base. A literature in which most results come from one collaborating network has not been subjected to the adversarial replication that gives a body of evidence its weight. The 2025 spinal cord injury study from an independent Chinese group [14] is a rare exception, and it is preclinical.

The Western trial base is absent, not merely limited. There is no MHRA, EMA or FDA assessment report to consult, no public regulatory review of a safety database, and no dossier that has been examined by a regulator applying the standards those agencies apply.

Preclinical neuroprotection translates badly. The rodent stroke literature summarised above sits in a field with a long and well-documented record of preclinical neuroprotective findings failing to reproduce in adequately powered human trials. The transcriptomic and protein-expression studies [9–12] describe molecular changes in a rat model; they are not evidence about clinical outcomes in people, and the studies themselves do not claim to be.

The two human imaging studies measure imaging endpoints. A difference in the volume of a resting-state network subcomponent [22] or in amygdala-temporal connectivity [23] is a neuroimaging observation in a small sample of healthy volunteers. It is not a cognitive outcome, and neither study reported one.

No long-term human safety data exist in the indexed literature. The studies identified are short, small, and were not designed or powered to detect uncommon adverse events. Absence of reported harm in studies of this size is not evidence of safety.

Material of uncertain provenance circulates. Vanhee and colleagues (2020) identified Semax among cognitive-enhancement research peptides recovered from seized pharmaceutical preparations, and developed analytical methodology specifically because controlling agencies were expected to encounter these compounds [24]. Any material obtained outside a documented supply chain should be treated as of unverified identity and content until it has been analysed.

Regulatory and standards position

United Kingdom. Semax holds no marketing authorisation from the MHRA. It is not an authorised medicinal product and no UK product licence exists for it in any presentation. It is not a controlled drug under the Misuse of Drugs Act 1971 and appears in no schedule of the Misuse of Drugs Regulations 2001. Its lawful position in the UK is as a laboratory chemical supplied for research use. Note that under the Human Medicines Regulations 2012 and MHRA Guidance Note 8, a substance can become a medicinal product by presentation on the strength of claims made about it, independently of what the molecule is — the classification follows the claim.

European Union. No centralised marketing authorisation from the EMA, and no product authorised through the decentralised or mutual recognition routes.

United States. Not approved by the FDA. It is not an approved drug substance and no approved product contains it.

Russian Federation. This is the one jurisdiction where the position differs. Semax is registered as a medicinal product in Russia and is marketed there in intranasal presentations. That registration is the origin of most of the clinical literature described above. A marketing authorisation in one jurisdiction confers no status in the UK, the EU or the US, and the assessment underlying it is not publicly available in the way a European Public Assessment Report or an FDA review would be.

Anti-doping. Semax is not named on the WADA Prohibited List. Two points qualify that, and both matter more than the bare statement.

First, the List is written by class as well as by name, so absence of a name is not a clearance. Section S2.2 prohibits corticotrophins and their releasing factors, naming corticorelin and tetracosactide. Semax is built on the ACTH(4-7) fragment, which lacks the region of the ACTH molecule responsible for corticotropic activity, so it is not a corticotrophin in the functional sense that subsection addresses — but that is an argument, not a ruling.

Second, section S0 prohibits substances with no current approval by any governmental regulatory health authority for human therapeutic use. Semax’s Russian registration is an approval by a governmental regulatory health authority, which on the plain wording places it outside S0 — while its absence of approval anywhere in the UK, EU or US is exactly the situation S0 was drafted to capture. The status is therefore genuinely unsettled rather than settled in either direction. Where the question arises under anti-doping rules, the only reliable answer is a written determination from the relevant national anti-doping organisation. This entry is not such a determination, nor is Global DRO output retrieved for a differently named product, nor is any supplier’s assertion.

Laboratory handling and safety

Semax should be handled as a biologically active research chemical of incompletely characterised toxicology. No comprehensive toxicological dataset is publicly available, and the correct posture in that situation is control by default rather than control proportionate to known hazard.

Personal protective equipment. Safety spectacles to EN 166, nitrile gloves and a fastened laboratory coat as the minimum. Weighing and any operation that could generate airborne powder — opening a lyophilised vial, transferring solid, sonicating an open vessel — belong in a fume hood or a powder-containment enclosure. Lyophilised peptide cakes are light and disperse easily; the dry-handling step is the highest-exposure operation in the workflow and is routinely underestimated because the quantities look trivial.

Reconstitution. Add diluent down the vial wall rather than directly onto the cake, and allow the solid to dissolve rather than forcing it. Vortexing and vigorous agitation introduce air-water interface and shear, both of which promote peptide degradation, and generate aerosol at the moment the vial is opened. Vent the vial deliberately if pressure has built up.

Spills. For dry powder, do not sweep or use compressed air — both re-aerosolise. Cover with a damp absorbent pad to suppress dust, collect, and wipe the area with a damp cloth followed by a detergent wash. For solution spills, absorb with pads, then wash the surface. Decontaminate reusable glassware by soaking in dilute sodium hypochlorite or by autoclaving; the amide backbone is not resistant to either.

Disposal. Peptide waste, contaminated consumables, expired stocks and unused reconstituted solution are chemical waste. Dispose through a licensed waste contractor in accordance with the Hazardous Waste Regulations and local waste policy. Do not discharge solutions to drain.

Record-keeping. Maintain, for each vial: supplier and batch or lot identifier, date received, storage location and temperature, date of reconstitution, identity and volume of diluent used, resulting nominal concentration, aliquot count, and the date and quantity of each withdrawal. Retain the certificate of analysis with the batch record and note the analytical method and detection wavelength it used, since as set out above a purity figure is only interpretable alongside the conditions that produced it. Where material is used in work intended for publication, the batch identifier and analytical characterisation should be recorded at the outset, not reconstructed afterwards.

References

1. Safarova ER, Shram SI, Zolotarev YA, Myasoedov NF. Effect of Semax peptide on survival of cultured rat pheochromocytoma cells during oxidative stress. Bulletin of Experimental Biology and Medicine, 2003; 135(3): 268–271. Model: in vitro (PC12 cells). PMID 12802399
2. Grivennikov IA, Dolotov OV, Zolotarev YA, Andreeva LA, Myasoedov NF, Leacher L, Black IB, Dreyfus CF. Effects of behaviorally active ACTH (4-10) analogue — Semax on rat basal forebrain cholinergic neurons. Restorative Neurology and Neuroscience, 2008; 26(1): 35–43. Model: in vitro (primary rat basal forebrain cultures). PMID 18431004
3. Novosadova EV, Arsenyeva EL, Antonov SA, Vanyushina YN, Malova TV, Komissarov AA, Illarioshkin SN, Khaspekov LG, Andreeva LA, Myasoedov NF, Tarantul VZ, Grivennikov IA. The use of human induced pluripotent stem cells for testing neuroprotective activity of pharmacological compounds. Biochemistry (Moscow), 2019; 84(11): 1296–1305. Model: in vitro (human iPSC-derived neurons). PMID 31760919
4. Dolotov OV, Seredenina TS, Levitskaya NG, Kamensky AA, Andreeva LA, Alfeeva LY, Nagaev IY, Zolotarev YA, Grivennikov IA, Engele Y, Myasoedov NF. The heptapeptide SEMAX stimulates BDNF expression in different areas of the rat brain in vivo. Doklady Biological Sciences, 2003; 391: 292–295. Model: rodent. PMID 14556513
5. Dolotov OV, Karpenko EA, Inozemtseva LS, Seredenina TS, Levitskaya NG, Rozyczka J, Dubynina EV, Novosadova EV, Andreeva LA, Alfeeva LY, Kamensky AA, Grivennikov IA, Myasoedov NF, Engele J. Semax, an analog of ACTH(4-10) with cognitive effects, regulates BDNF and trkB expression in the rat hippocampus. Brain Research, 2006; 1117(1): 54–60. Model: rodent. PMID 16996037
6. Shadrina M, Kolomin T, Agapova T, Agniullin Y, Shram S, Slominsky P, Lymborska S, Myasoedov N. Comparison of the temporary dynamics of NGF and BDNF gene expression in rat hippocampus, frontal cortex, and retina under Semax action. Journal of Molecular Neuroscience, 2010; 41(1): 30–35. Model: rodent. PMID 19662538
7. Romanova GA, Silachev DN, Shakova FM, Kvashennikova YN, Viktorov IV, Shram SI, Myasoedov NF. Neuroprotective and antiamnesic effects of Semax during experimental ischemic infarction of the cerebral cortex. Bulletin of Experimental Biology and Medicine, 2006; 142(6): 663–666. Model: rodent. PMID 17603664
8. Stavchansky VV, Yuzhakov VV, Botsina AY, Skvortsova VI, Bondurko LN, Tsyganova MG, Limborska SA, Myasoedov NF, Dergunova LV. The effect of Semax and its C-end peptide PGP on the morphology and proliferative activity of rat brain cells during experimental ischemia: a pilot study. Journal of Molecular Neuroscience, 2011; 45(2): 177–185. Model: rodent. PMID 20617398
9. Medvedeva EV, Dmitrieva VG, Povarova OV, Limborska SA, Skvortsova VI, Myasoedov NF, Dergunova LV. The peptide semax affects the expression of genes related to the immune and vascular systems in rat brain focal ischemia: genome-wide transcriptional analysis. BMC Genomics, 2014; 15: 228. Model: rodent. PMID 24661604
10. Medvedeva EV, Dmitrieva VG, Limborska SA, Myasoedov NF, Dergunova LV. Semax, an analog of ACTH(4-7), regulates expression of immune response genes during ischemic brain injury in rats. Molecular Genetics and Genomics, 2017; 292(3): 635–653. Model: rodent. PMID 28255762
11. Filippenkov IB, Stavchansky VV, Denisova AE, Yuzhakov VV, Sevan’kaeva LE, Sudarkina OY, Dmitrieva VG, Gubsky LV, Myasoedov NF, Limborska SA, Dergunova LV. Novel insights into the protective properties of ACTH(4-7)PGP (Semax) peptide at the transcriptome level following cerebral ischaemia-reperfusion in rats. Genes (Basel), 2020; 11(6): 681. Model: rodent. PMID 32580520
12. Sudarkina OY, Filippenkov IB, Stavchansky VV, Denisova AE, Yuzhakov VV, Sevan’kaeva LE, Valieva LV, Remizova JA, Dmitrieva VG, Gubsky LV, Myasoedov NF, Limborska SA, Dergunova LV. Brain protein expression profile confirms the protective effect of the ACTH(4-7)PGP peptide (Semax) in a rat model of cerebral ischemia-reperfusion. International Journal of Molecular Sciences, 2021; 22(12): 6179. Model: rodent. PMID 34201112
13. Glazova NY, Manchenko DM, Volodina MA, Merchieva SA, Andreeva LA, Kudrin VS, Myasoedov NF, Levitskaya NG. Semax, synthetic ACTH(4-10) analogue, attenuates behavioural and neurochemical alterations following early-life fluvoxamine exposure in white rats. Neuropeptides, 2021; 86: 102114. Model: rodent. PMID 33418449
14. Liu R, Chen Y, Huang H, Li X, Lv J, Jiang L, Jiang H, Wu C, Chen W, Xu H, Zhu Z, Cai H, Xiao J, Yin L, Ni W. Semax peptide targets the µ opioid receptor gene Oprm1 to promote deubiquitination and functional recovery after spinal cord injury in female mice. British Journal of Pharmacology, 2025; 182(22): 5489–5516. Model: rodent. PMID 40692165
15. Gusev EI, Skvortsova VI, Miasoedov NF, Nezavibat’ko VN, Zhuravleva EIu, Vanichkin AV. Effectiveness of semax in acute period of hemispheric ischemic stroke (a clinical and electrophysiological study). Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 1997; 97(6): 26–34. Russian language. Model: human (30 treated, 80 controls). PMID 11517472
16. Polunin GS, Nurieva SM, Baiandin DL, Sheremet NL, Andreeva LA. Evaluation of therapeutic effect of new Russian drug semax in optic nerve disease. Vestnik oftalmologii, 2000; 116(1): 15–18. Russian language. Model: human. PMID 10741256
17. Kurysheva NI, Shpak AA, Ioĭleva EE, Galanter LI, Nagornova ND, Shubina NIu, Shlyshalova NN. Semax in the treatment of glaucomatous optic neuropathy in patients with normalized ophthalmic tone. Vestnik oftalmologii, 2001; 117(4): 5–8. Russian language. Model: human. PMID 11569188
18. Ivanikov IO, Brekhova ME, Samonina GE, Myasoedov NF, Ashmarin IP. Therapy of peptic ulcer with semax peptide. Bulletin of Experimental Biology and Medicine, 2002; 134(1): 73–74. Model: human. PMID 12459874
19. Gusev EI, Skvortsova VI, Chukanova EI. Semax in prevention of disease progress and development of exacerbations in patients with cerebrovascular insufficiency. Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 2005; 105(2): 35–40. Russian language. Model: human (187 patients). PMID 15792140
20. Serdiuk AV, Levitskiĭ GN, Miasoedov NF, Skvortsova VI. The study of chronic partial denervation and quality of life in patients with motor neuron disease treated with semax. Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 2007; 107(4): 29–39. Russian language. Indexed publication type: Randomized Controlled Trial. Model: human. PMID 18379501
21. Gusev EI, Martynov MY, Kostenko EV, Petrova LV, Bobyreva SN. The efficacy of semax in the treatment of patients at different stages of ischemic stroke. Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 2018; 118(3, issue 2): 61–68. Russian language. Model: human (110 patients). PMID 29798983
22. Lebedeva IS, Panikratova YR, Sokolov OY, Kupriyanov DA, Rumshiskaya AD, Kost NV, Myasoedov NF. Effects of Semax on the default mode network of the brain. Bulletin of Experimental Biology and Medicine, 2018; 165(5): 653–656. Model: human (24 healthy volunteers, resting-state fMRI). PMID 30225715
23. Panikratova YR, Lebedeva IS, Sokolov OY, Rumshiskaya AD, Kupriyanov DA, Kost NV, Myasoedov NF. Functional connectomic approach to studying Selank and Semax effects. Doklady Biological Sciences, 2020; 490(1): 9–11. Model: human (52 healthy participants, resting-state fMRI). PMID 32342318
24. Vanhee C, Francotte A, Janvier S, Deconinck E. The occurrence of putative cognitive enhancing research peptides in seized pharmaceutical preparations: an incentive for controlling agencies to prepare for future encounters of the kind. Drug Testing and Analysis, 2020; 12(3): 371–381. Model: analytical (LC-MS/MS characterisation of seized preparations). PMID 31667971

Research use only

This entry is a technical and bibliographic reference about a laboratory chemical. It is not medical advice, not a protocol, and not a recommendation to use this substance in any way.

Semax is supplied for laboratory research use only. It is not authorised as a medicine in the United Kingdom, the European Union or the United States, and it is not for human or veterinary use, for use in food, or for any diagnostic or therapeutic application. It must be handled only by trained personnel in an appropriate laboratory environment, under local risk assessment and COSHH arrangements.

The literature summarised above is reported as literature. A description of what a study examined and reported is a statement about that study, and is not a claim that this substance has any effect in humans, that it is safe, or that it is suitable for any purpose. Nothing here should be read as suggesting otherwise.