Semax

Semax in brief

Semax is a synthetic heptapeptide, Met-Glu-His-Phe-Pro-Gly-Pro, made by joining residues 4 to 7 of adrenocorticotropic hormone to a Pro-Gly-Pro tail, with no other modification. It was designed in Moscow in the 1980s and has been in Russian medical use for decades. Despite its common label as an ACTH(4-10) analogue, an early report found neither steroidogenic nor melanocyte-stimulating activity. Its best-defined chemistry is an amino-terminal motif that binds copper(II) very tightly. Saturable nanomolar binding to rat forebrain membranes has been reported by one group, but no receptor has been identified, and most of the literature comes from one Moscow institute.^[1,2,3,4,5]

Semax regulatory status

Semax is registered as a medicine in the Russian Federation. No FDA, EMA or Health Canada marketing authorisation was found in Drugs@FDA, the EMA medicines database or the Health Canada Drug Product Database (searched November 2026), ClinicalTrials.gov holds no registered study with it as an intervention, and it is not named on the WADA 2026 Prohibited List. The FDA's compounding safety-risk page lists semax (heptapeptide) among bulk substances previously in category 2 whose nominations were withdrawn by the nominators, and keeps the agency's stated concern: a risk of immunogenicity due to the potential for aggregation and peptide-related impurities, and no, or limited, safety-related information, so that the agency lacks sufficient information to know whether it would cause harm in humans (page current as of 22 April 2026).^{[6,7,8,9,10,11,12]}

Semax at a glance

• Status: in Russian medical use for decades and authorised nowhere else. No FDA, EMA or Health Canada marketing authorisation was found, ClinicalTrials.gov holds no registered study with it as an intervention, and it is not named on the WADA 2026 Prohibited List. The FDA's compounding safety-risk page lists semax (heptapeptide) among bulk substances whose nominations were withdrawn, with the agency's stated concern a risk of immunogenicity from aggregation and peptide-related impurities together with no, or limited, safety-related information.^{[3,7,8,9,11,10,12]}
• What the literature is, counted: of the 52 works counted for this entry, one used human participants, a placebo-controlled resting-state functional MRI study in 52 healthy volunteers. The rest is rat whole-animal and tissue work, cell culture, and solution chemistry. Almost all of the binding, degradation, transcriptome and behavioural work comes from one Moscow institute and its collaborators; the independent contributions are a coordination-chemistry series from an Italian group, a control laboratory's analysis of preparations, and two papers from outside that network.^{[13,4,14,15,16,17]}
• It is a chimera by design: residues 4 to 7 of corticotropin joined to a Pro-Gly-Pro tail chosen for proteolytic stability. Comparative work found Pro-Gly-Pro and two of its extensions considerably more stable to proteolysis than the heptapeptide, against leucine aminopeptidase, brain microsomal fractions and rat blood, so the tail outlasts the molecule it was added to stabilise.^[18,19]
• The commonest name for it, ACTH(4-10) analogue, is a numbering relationship rather than a chemical one. ACTH(4-10) is MEHFRWG; this molecule drops Arg-Trp-Gly, which is where the melanocortin receptor pharmacophore sits, and the earliest record reports neither steroidogenic nor melanocyte-stimulating activity.^[20,2]
• Saturable, calcium-dependent, reversible binding to rat forebrain membranes has been reported twice by the same group, with a dissociation constant near 2.4 nanomolar and a low site density of about 33.5 femtomoles per milligram of protein. The site has never been identified as a molecular entity.^[21,5]
• Its best-defined chemistry is coordination chemistry: the free amine, two backbone amide nitrogens and the His3 imidazole form an amino-terminal copper and nickel binding motif holding copper(II) about ten orders of magnitude more tightly than zinc(II).^[14,4,22]

What is Semax?

Semax is a short synthetic peptide designed in Moscow in the 1980s, in a programme that set out to keep the behavioural activity attributed to the N-terminal part of adrenocorticotropic hormone while leaving the hormone's endocrine actions behind. Human corticotropin runs SYSMEHFRWGKPV at its N-terminus; this molecule keeps Met-Glu-His-Phe, the residues numbered 4 to 7, and carries Pro-Gly-Pro in place of the next three. A 1986 report is the earliest record found of the separation it was built for: the heptapeptide showed no steroidogenic and no melanocyte-stimulating activity in that work, where ACTH(5-10) did.^[20,2,3]

The appended tripeptide is the design's second idea. The same group describes a family of Pro-Gly-Pro-containing peptides as chimeric constructs, joining a fragment of one natural regulatory peptide to a stabilising glyproline tail, with Selank as the other well-known member.^[18]

Side by side with Selank, the other well-known member of the same series, the differences are easy to state. Parent fragment: corticotropin 4 to 7 here, against tuftsin, the blood tetrapeptide Thr-Lys-Pro-Arg, for Selank. Length: seven residues each, both ending in the same appended Pro-Gly-Pro, so the first four residues are where they differ and they differ completely. Sequence and composition: Met-Glu-His-Phe-Pro-Gly-Pro, which carries a methionine, a histidine and a phenylalanine and so has both a sulfur atom and an aromatic ring; Selank is Thr-Lys-Pro-Arg-Pro-Gly-Pro, with two basic side chains, three prolines and no histidine, no methionine and no sulfur anywhere. Best-defined chemistry: an amino-terminal copper and nickel binding motif here, which Selank cannot form because the side-chain donors are absent; for Selank it is the degradation pathway. Main assay types: rat ischaemia and learning models, transcriptome and proteome profiles, membrane radioligand binding and serum peptidase assays here; rodent anxiety-related behaviour, transcript arrays and the same peptidase work for Selank. Both have a resting-state functional MRI study in healthy volunteers, from the same group and the same cohort. Neither has an identified receptor, and the shared C-terminal tripeptide has activity of its own, so a result obtained with one is not evidence about the other.^{[18,23,14,13,24]}

Its literature is unusual in shape. More than two hundred PubMed records mention it, concentrated in Russian-language journals and the Doklady series, and a large fraction are organism-level rat studies or clinical reports from a programme in which the peptide has been in Russian medical use for decades. The one human study found is a resting-state imaging measurement rather than a molecular one. Independent molecular work comes mostly from a single Italian coordination-chemistry group, and one European medicines control laboratory identified the peptide in two preparations it examined and built a validated mass-spectrometric method for it.^[3,13,4,15]

The written chemistry is settled and the pharmacology is not. Sequence, formula, mass and CAS number agree across PubChem, the FDA substance register and the primary papers. No receptor has been identified, no affinity at any named receptor has been published, and no three-dimensional structure of the peptide exists in any public archive.^[1,25,26]

Semax structure and sequence

The chain reads Met1-Glu2-His3-Phe4-Pro5-Gly6-Pro7. Methionine at position 1 supplies a thioether sulfur beside the free terminal amine, glutamate at 2 is the only acidic side chain apart from the C-terminal carboxylate, and histidine at 3 supplies the imidazole. Phenylalanine at 4 is the one aromatic residue, so the peptide absorbs usefully near 254 nanometres but has no tryptophan and therefore no strong 280 nanometre chromophore, and the degradation work reads the chromatograms at 220 and 254 nanometres. PubChem computes 21 rotatable bonds, eight hydrogen-bond donors and an XLogP of -2.8 across 57 heavy atoms: a small, flexible, strongly hydrophilic molecule.^[1,21]

Met-Glu-His is not an arbitrary opening. A free alpha-amino group with histidine in the third position is the amino-terminal copper and nickel binding motif, and this peptide is explicitly identified as carrying one. Titration found three copper(II) species, two minor ones between about pH 3.6 and 5 and one predominant from pH 5 upward whose donor set is four nitrogens in a plane: the terminal amine, two deprotonated backbone amide nitrogens and the imidazole. The conditional dissociation constant at pH 7.4 is about 1.3 times ten to the minus fifteen molar, against about 1.8 times ten to the minus five molar for zinc(II). Acetylating the terminal amine removes one of the four nitrogen donors: the chromophore becomes a distorted CuN3O with a weak apical contact from the methionine sulfur, the formal redox potential shifts positive, and the complex reacts with ascorbate where the free-amine complex does not.^[14,4,22]

There is no three-dimensional view to show, and that is a property of the molecule rather than a gap in the search. Two PDB searches found nothing, by name and by sequence motif, and PubChem holds no computed conformer. No NMR or circular dichroism study of the peptide was found either, so the copper donor set above is the nearest thing to a structure here and it is a solution assignment. The molecule also stops being itself during an experiment, because peptidases clip Met-Glu from one end and Gly-Pro from the other.^[1,27,28]

Every chiral residue is the L enantiomer and the single glycine at position 6 is achiral, so PubChem reports six defined atom stereocentres and none undefined for CID 9811102. There is no cysteine, therefore no disulfide and no free thiol; the only sulfur is the methionine thioether at position 1, which is a coordinating atom rather than a cross-link. The chain is linear and uncyclised, with no lipidation, no PEG, no glycosylation and no amidation. Two of the seven residues are proline, at positions 5 and 7, which removes two backbone amide hydrogens and constrains the C-terminal end locally. The free N-terminal amine is part of the molecule's identity rather than an incidental feature: with histidine at position 3 it completes an amino-terminal copper and nickel binding motif, and acetylating it changes the coordination chemistry outright.^[1,22,14]

What studies on Semax show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

Semax compared with Selank and Melanotan II

Four things about the 3 compounds most often read beside it, on axes that can be checked: what kind of substance it is, its formula and mass, what public records settle about which substance it is, and the strongest three-dimensional evidence that exists for it. Every figure is the one stated on that compound's own page, which is where it is cited, so the two can never disagree. The table compares no effect, no potency and nothing a compound has been reported to do, and these compounds are not alternatives to one another.

Three molecular handles, and no identified receptor between them

The first handle is a membrane binding site: the saturable, reversible, calcium-dependent, low-nanomolar binding to rat forebrain membranes reported twice by the same group and quantified above, with the two main fragments showing their own sites with distinguishable characteristics. Nothing has identified the molecule those sites belong to. Melanocortin receptors are the obvious candidate on the strength of the name, and a targeted search for the peptide alongside any melanocortin receptor subtype returned nothing resembling a receptor assay, in either direction; the chemistry points away from them, because the His-Phe-Arg-Trp core those receptors read is exactly what the Pro-Gly-Pro tail replaced. One 2025 paper nominates the mu-opioid receptor by network pharmacology and docking rather than by a binding experiment, with no affinity figure and no receptor-null control.^{[21,5,26,32,2,16]}

The second handle is coordination chemistry, and it is the best-defined thing about the molecule. The amino-terminal motif holds copper(II) in a four-nitrogen planar donor set at physiological pH. In buffer that is tight enough to take copper(II) off amyloid-beta and silence the metal's redox cycling. The copper-free comparison in the same assay series is what keeps this a statement about the metal rather than about the two peptides: at an equimolar ratio the peptide did not significantly perturb any kinetic parameter of amyloid-beta fibril formation in buffer, and the reduction in fibre formation those authors report is concentration dependent and largest in the presence of copper. What it does not do is account for the rest of the literature: the measurements use defined buffer at micromolar concentrations of both peptide and metal, and nothing has shown the peptide meets free copper in a tissue.^[14,33,4,22]

The third handle is that the molecule does not stay itself, which makes the fragments part of any mechanism. Serum work attributes most hydrolysis to aminopeptidases, removing Met1 then Glu2, with a contribution from angiotensin-converting enzyme, and in a tritium-tracer study about 80 per cent of the labelled material recovered from rat brain was still intact peptide two minutes after delivery, with Pro-Gly-Pro predominating thereafter. The originating group treats parent and fragments as one functional set, which it calls a synacton; that is a hypothesis, and the fragments are not equivalent, since Pro-Gly-Pro changed neither deficit scores nor mortality in a rat ischaemia model where the full peptide did, yet drives neurotrophin transcription on its own. Position 1 is where the structure-activity work converges: replacing Met1 with glycine, threonine or alanine abolished activity in rat learning tests and removed it in a nociceptive test, while lysine or a glucuronic acid cap preserved it, and those same substitutions made the peptide more resistant to aminopeptidase. Stability and activity pull in opposite directions at the one residue that also completes the copper site.^{[34,35,27,28,24,36,37,38,39]}

Everything past those three handles is response measurement rather than mechanism, and it is worth separating from them. In cerebral ischaemia models the readouts are genome-wide transcript profiles, including immune, vascular and proinflammatory transcript sets, and a brain protein expression profile; in glial culture and in rat brain they are neurotrophin and trkB transcript and protein levels, measured in one study against the Pro-Gly-Pro comparator. The electrophysiology and signalling measurements are currents at GABA, glycine and AMPA receptors in isolated neurons, direct and delayed effects on the GABA receptor system, intracellular calcium fluctuation frequency, a nitric oxide endpoint in cortex against a glycine comparator, and striatal 5-HIAA as an index of serotonin turnover. Each of these is a change measured after exposure in a named species or preparation. None of them identifies an initiating interaction, which is why the three items above are described as handles rather than as a mechanism.^{[40,41,42,36,43,31,44,45,46,29,47,48,49,50,51]}

What is still unknown about Semax

No target, after more than two hundred papers. The binding data establish that rat forebrain membranes carry a small number of high-affinity sites; they do not say what those sites are, and no paper found reports an affinity at a named, cloned receptor. The literature measures downstream readouts instead, which is why mechanism sections in this field end in a candidate rather than an answer, and both existing candidates, a docking-derived mu-opioid nomination and a transthyretin hypothesis built from array data, are explicitly weak.^{[26,16,52,53]}

A concentration gap runs through the literature and is rarely acknowledged. Binding is nanomolar. The cell and tissue experiments are mostly micromolar to millimolar: 1 micromolar for the ion-current and calcium work, 10 to 100 micromolar in the synapse and glutamate-challenge studies, about 10 micromolar for inhibition of serum enkephalin-degrading activity, and millimolar for the arachidonoyl conjugates. A result obtained four orders of magnitude above a measured dissociation constant cannot be attributed to the site that constant describes, and no paper found reconciles the two.^{[21,29,54,55,23,56]}

Replication is mostly internal. Almost all of the binding, degradation, transcriptome and behavioural work comes from one Moscow institute and its collaborators, often sharing authors across decades, and much of it sits in Russian-language journals where only an English abstract is indexed. The independent contributions found here are a coordination-chemistry series from one Italian group, a Belgian control laboratory's identification of the peptide in material it examined, a 2025 Chinese spinal-cord-injury paper, and a screening panel that measured it beside Selank and Pro-Gly-Pro.^{[4,14,15,16,17]}

Three structural questions have no answer. There is no experimentally determined conformation of the free peptide, in solution or bound. There is no structure of the copper complex whose donor set is otherwise well argued. The single independent analysis identified the peptide in two preparations examined by a control laboratory, while the cell-level work uses defined peptide. The published chemistry describes the free peptide with free termini, no salt form is registered, and a mass figure for it should not be read across to one. A fourth, smaller point belongs with them: the identifier set most widely reproduced for this peptide, including the InChIKey and ChemSpider record carried by a reference encyclopedia, describes the same constitution with the His3 stereocentre left unspecified, so a database lookup that follows it does not land on the fully defined all-L record. There is also no assigned ATC code: the N06BX prefix that circulates for this peptide is a group heading, and the WHO ATC index lists no entry for it under that group.^{[1,4,15,57,25,58,59,60]}

Key papers on Semax

1. Semax, an analogue of adrenocorticotropin (4-10), binds specifically and increases levels of brain-derived neurotrophic factor protein in rat basal forebrain

   Dolotov OV, Karpenko EA, Seredenina TS, Inozemtseva LS, Levitskaya NG, Zolotarev YA, Kamensky AA, Grivennikov IA, Engele J, Myasoedov NF (2006), Journal of Neurochemistry · Radioligand binding and protein assay

   The clearest single account of the binding evidence, with the dissociation constant and site density in an English-language journal, and a protein measurement in the same paper. It is also the paper whose title fixed the misleading ACTH(4-10) label in the English literature.

2. Semax, a Copper Chelator Peptide, Decreases the Cu(II)-Catalyzed ROS Production and Cytotoxicity of aβ by Metal Ion Stripping and Redox Silencing

   Tomasello MF, Di Rosa MC, Naletova I, Sciacca MFM, Giuffrida A, Maccarrone G, Attanasio F (2025), Bioinorganic Chemistry and Applications · Solution coordination chemistry with cellular readout

   Open access, and the best entry point to the coordination chemistry: it names the amino-terminal copper and nickel motif, gives the copper and zinc affinities side by side, and states its own limit about Cu(I) rather than leaving it to the reader.

3. Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties

   Magrì A, Tabbì G, Giuffrida A, Pappalardo G, Satriano C, Naletova I, Nicoletti VG, Attanasio F (2016), Journal of Inorganic Biochemistry · Comparative coordination chemistry

   Read second for the chemistry. By comparing the free and acetylated peptides it shows exactly which atom completes the copper site, which is the sharpest structure-function result anywhere in this literature.

4. Degradation of the ACTH(4-10) analog Semax in the presence of rat basal forebrain cell cultures and plasma membranes

   Zolotarev YA, Dolotov OV, Inozemtseva LS, Dadayan AK, Dorokhova EM, Andreeva LA, Alfeeva LY, Grivennikov IA, Myasoedov NF (2006), Amino Acids · Isotope-labelled degradation analysis

   Read before trusting any experiment lasting more than a few minutes. It shows the molecule being clipped at both ends into pentapeptides, with different product patterns in glial and neuronal cultures.

5. C-terminal Pro-Gly-Pro tripeptide in contrast to full-length neuropeptide semax exhibits no neuroprotective effect in experimental cerebral ischemia

   Fadyukova OE, Kadi A, Bai O, Andzhusheva GM, Koshelev VB (2005), Bulletin of Experimental Biology and Medicine · Rat model comparison of peptide and fragment

   One page that stops the commonest error in this field, which is treating the parent peptide and its Pro-Gly-Pro fragment as the same agent.

6. [Effect of modification of the N-terminal region of molecule on the expression of neotropic effect of semax analogues]

   Glazova NIu, Sebentsova EA, Levitskaia NG, Andreeva LA, Alfeeva LIu, Kamenskiĭ AA, Miasoedov NF (2005), Izvestiia Akademii Nauk, Seriia Biologicheskaia · Structure-activity series in rat learning tests

   The position-1 structure-activity series, and the place where the tension between proteolytic stability and activity becomes visible: the substitutions that make the peptide last longer are the ones that cost it its activity.

7. Functional Connectomic Approach to Studying Selank and Semax Effects

   Panikratova YR, Lebedeva IS, Sokolov OY, Rumshiskaya AD, Kupriyanov DA, Kost NV, Myasoedov NF (2020), Doklady Biological Sciences · placebo-controlled resting-state functional MRI

   The only study found in which the peptide was given to human participants against placebo, and a short read on how little a resting-state connectivity measurement settles.

8. Novel Insights into the Protective Properties of ACTH((4-7))PGP (Semax) Peptide at the Transcriptome Level Following Cerebral Ischaemia-Reperfusion in Rats

   Filippenkov IB, Stavchansky VV, Denisova AE, Yuzhakov VV, Sevan'kaeva LE, Sudarkina OY, Dmitrieva VG, Gubsky LV, Myasoedov NF, Limborska SA, Dergunova LV (2020), Genes · Genome-wide RNA sequencing

   Representative of the largest strand of the modern literature, genome-scale response profiling in a rat occlusion model, and a fair illustration of what that strand can and cannot establish.

9. 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

   Vanhee C, Francotte A, Janvier S, Deconinck E (2020), Drug Testing and Analysis · Analytical identification in preparations examined by a control laboratory

   The one identification of this peptide in supplied material by a laboratory independent of the originating programme, with a validated mass-spectrometric method.

References

1. 1.PubChem. Semax, compound summary CID 9811102. PubChem, National Center for Biotechnology Information. source · database record
2. 2.Ponomareva-Stepnaia MA, Porunkevich EA, Skuin'sh AA, Nezavibat'ko VN, Ashmarin IP. (1986). [Hormonal activity of the ACTH(4-10) analog--a prolonged-action stimulant of learning]. Biulleten' Eksperimental'noi Biologii i Meditsiny. 101:267-268. PMID 3006824 · abstract only
3. 3.Asmarin IP, Nezavibat'ko VN, Miasoedov NF, Kamenskiĭ AA, Grivennikov IA, Ponomareva-Stepnaia MA, Andreeva LA, Kaplan AIa, Koshelev VB, Riasina TV. (1997). [A nootropic adrenocorticotropin analog 4-10-semax (l5 years experience in its design and study)]. Zhurnal Vysshei Nervnoi Deiatel'nosti Imeni I P Pavlova. 47:420-430. PMID 9173745 · abstract only
4. 4.Tabbì G, Magrì A, Giuffrida A, Lanza V, Pappalardo G, Naletova I, Nicoletti VG, Attanasio F, Rizzarelli E. (2015). Semax, an ACTH4-10 peptide analog with high affinity for copper(II) ion and protective ability against metal induced cell toxicity. Journal of Inorganic Biochemistry. 142:39-46. doi:10.1016/j.jinorgbio.2014.09.008 · abstract only
5. 5.Dolotov OV, Karpenko EA, Seredenina TS, Inozemtseva LS, Levitskaya NG, Zolotarev YA, Kamensky AA, Grivennikov IA, Engele J, Myasoedov NF. (2006). Semax, an analogue of adrenocorticotropin (4-10), binds specifically and increases levels of brain-derived neurotrophic factor protein in rat basal forebrain. Journal of Neurochemistry. 97 Suppl 1:82-86. doi:10.1111/j.1471-4159.2006.03658.x · abstract only
6. 6.Deigin VI, Poluektova EA, Beniashvili AG, Kozin SA, Poluektov YM. (2022). Development of Peptide Biopharmaceuticals in Russia. Pharmaceutics. 14(4):716. doi:10.3390/pharmaceutics14040716 · full text read
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12. 12.U.S. Food and Drug Administration. (2026). Certain Bulk Drug Substances for Use in Compounding that May Present Significant Safety Risks (content current as of 22 April 2026). U.S. Food and Drug Administration, Human Drug Compounding. source · full text read
13. 13.Panikratova YR, Lebedeva IS, Sokolov OY, Rumshiskaya AD, Kupriyanov DA, Kost NV, Myasoedov NF. (2020). Functional Connectomic Approach to Studying Selank and Semax Effects. Doklady Biological Sciences. 490:9-11. doi:10.1134/S001249662001007X · abstract only
14. 14.Tomasello MF, Di Rosa MC, Naletova I, Sciacca MFM, Giuffrida A, Maccarrone G, Attanasio F. (2025). Semax, a Copper Chelator Peptide, Decreases the Cu(II)-Catalyzed ROS Production and Cytotoxicity of aβ by Metal Ion Stripping and Redox Silencing. Bioinorganic Chemistry and Applications. 2025:4226220. doi:10.1155/bca/4226220 · full text read
15. 15.Vanhee C, Francotte A, Janvier S, Deconinck E. (2020). 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. 12:371-381. doi:10.1002/dta.2717 · abstract only
16. 16.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. (2025). 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. 182:5489-5516. doi:10.1111/bph.70122 · abstract only
17. 17.Kobylyanskii AG, Zolotarev YA, Andreeva LA, Grivennikov IA, Myasoedov NF. (2017). Studying the Toxic Effects of Some Biologically Active Peptides on the Model of Mouse Embryonic Stem Cells. Bulletin of Experimental Biology and Medicine. 163:731-736. doi:10.1007/s10517-017-3891-y · abstract only
18. 18.Ashmarin IP, Samonina GE, Lyapina LA, Kamenskii AA, Levitskaya NG, Grivennikov IA, Dolotov OV, Andreeva LA, Myasoedov NF. (2005). Natural and hybrid ("chimeric") stable regulatory glyproline peptides. Pathophysiology. 11:179-185. doi:10.1016/j.pathophys.2004.10.001 · abstract only
19. 19.Shevchenko KV, V'iunova TV, Nagaev IIu, Andreeva LA, Miasoedov NF. (2013). [Proteolysis of simple glyprolines by leucine aminopeptidase and enzymes from nasal slime, brain membranes, and rat blood]. Bioorganicheskaia Khimiia. 39:320-325. doi:10.1134/s1068162013030151 · abstract only
20. 20.UniProt Consortium. P01189, Pro-opiomelanocortin, Homo sapiens. UniProtKB. source · database record
21. 21.Dolotov OV, Zolotarev IuA, Dorokhova EM, Andreeva LA, Alfeeva LIu, Grivennikov IA, Miasoedov NF. (2004). [The binding of Semax, ACTH 4-10 heptapeptide, to plasma membranes of the rat forebrain basal nuclei and its biodegradation]. Bioorganicheskaia Khimiia. 30:241-246. doi:10.1023/b:rubi.0000030127.46845.f0 · abstract only
22. 22.Magrì A, Tabbì G, Giuffrida A, Pappalardo G, Satriano C, Naletova I, Nicoletti VG, Attanasio F. (2016). Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties. Journal of Inorganic Biochemistry. 164:59-69. doi:10.1016/j.jinorgbio.2016.08.013 · abstract only
23. 23.Kost NV, Sokolov OIu, Gabaeva MV, Grivennikov IA, Andreeva LA, Miasoedov NF, Zozulia AA. (2001). [Semax and selank inhibit the enkephalin-degrading enzymes from human serum]. Bioorganicheskaia Khimiia. 27:180-183. doi:10.1023/a:1011373002885 · abstract only
24. 24.Fadyukova OE, Kadi A, Bai O, Andzhusheva GM, Koshelev VB. (2005). C-terminal Pro-Gly-Pro tripeptide in contrast to full-length neuropeptide semax exhibits no neuroprotective effect in experimental cerebral ischemia. Bulletin of Experimental Biology and Medicine. 139:421-423. doi:10.1007/s10517-005-0311-5 · abstract only
25. 25.US Food and Drug Administration, Global Substance Registration System. ACTH (4-7), PRO-GLY-PRO-, substance record UNII I5FAL2585H. FDA GSRS. source · database record
26. 26.Vyunova TV, Andreeva LA, Shevchenko KV, Myasoedov NF. (2017). Synacton and individual activity of synthetic and natural corticotropins. Journal of Molecular Recognition. 30. doi:10.1002/jmr.2597 · abstract only
27. 27.Zolotarev YA, Dolotov OV, Inozemtseva LS, Dadayan AK, Dorokhova EM, Andreeva LA, Alfeeva LY, Grivennikov IA, Myasoedov NF. (2006). Degradation of the ACTH(4-10) analog Semax in the presence of rat basal forebrain cell cultures and plasma membranes. Amino Acids. 30:403-408. doi:10.1007/s00726-006-0328-8 · abstract only
28. 28.Shevchenko KV, Nagaev IIu, Alfeeva LIu, Andreeva LA, Kamenskiĭ AA, Levitskaia NG, Shevchenko VP, Grivennikov IA, Miasoedov NF. (2006). [Kinetics of Semax penetration into the brain and blood of rats after its intranasal administration]. Bioorganicheskaia Khimiia. 32:64-70. doi:10.1134/s1068162006010055 · abstract only
29. 29.Sharonova IN, Bukanova YV, Myasoedov NF, Skrebitskii VG. (2018). Modulation of GABA- and Glycine-Activated Ionic Currents with Semax in Isolated Cerebral Neurons. Bulletin of Experimental Biology and Medicine. 164:612-616. doi:10.1007/s10517-018-4043-8 · abstract only
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31. 31.Filippenkov IB, Stavchansky VV, Denisova AE, Yuzhakov VV, Sevan'kaeva LE, Sudarkina OY, Dmitrieva VG, Gubsky LV, Myasoedov NF, Limborska SA, Dergunova LV. (2020). Novel Insights into the Protective Properties of ACTH((4-7))PGP (Semax) Peptide at the Transcriptome Level Following Cerebral Ischaemia-Reperfusion in Rats. Genes. 11:681. doi:10.3390/genes11060681 · abstract only
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