This is a working overview of ACTH analog, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2026-01-22. Anything still debated is marked as such rather than presented as settled.
Semax binds to melanocortin receptors and is thought to influence neuronal survival and plasticity rather than to act through the adrenal axis. Laboratory work has shown increased expression of brain-derived neurotrophic factor and nerve growth factor in treated tissue. Changes in c-Fos, a marker of neuronal activation, have also been reported. Because the peptide is rapidly degraded by peptidases, its effects are generally attributed to downstream signaling cascades rather than to sustained receptor occupancy.
Published studies are dominated by animal models of stroke, ischemia, and cognitive impairment, with a smaller number of human trials conducted in Russia. Many of the human reports are small, single-center, and published in Russian-language journals, which limits independent scrutiny. Outcome measures vary between studies and often rely on clinician-rated scales rather than objective biomarkers. Systematic reviews have noted the methodological weaknesses and called for larger, preregistered trials before firm conclusions can be drawn.
Clinical reports describe use in ischaemic stroke, transient ischaemic attack, optic nerve conditions, and cognitive complaints, but most of these studies are small and were conducted in a single region. Systematic reviews have generally described the evidence base as limited in size and variable in methodological quality. Randomised controlled data suitable for international regulatory assessment are scarce. As a result, major treatment guidelines outside Russia do not include the peptide, and interest in it remains largely research-driven rather than routine clinical.
Semax is a synthetic heptapeptide with the sequence Met-Glu-His-Phe-Pro-Gly-Pro. It is described in the literature as an analogue of the ACTH(4–10) fragment, a short N-terminal portion of adrenocorticotropic hormone that retains some neurotropic activity without the full hormonal effects of the parent peptide. The molecule carries a methionine residue at the N-terminus and two proline residues near the C-terminus, features that shape both its interactions with receptor systems and its chemical stability. The free peptide corresponds to the formula C37H51N9O10S and a molecular mass near 813.9 Da.
The compound was developed in the 1980s at the Institute of Molecular Genetics in Moscow, where it emerged from research on short ACTH fragments and their effects on the central nervous system. Russian pharmaceutical listings describe it as a nootropic and neuroprotective agent, most often formulated as nasal drops. It is not a marketed medicine in the United States or the European Union, and no pharmacopoeial monograph covers it. Consequently, most published clinical experience with the substance originates from a small number of research centres, mainly in Russia and neighbouring countries.
| Property | Value | Notes |
|---|---|---|
| Appearance | White lyophilized powder | Typical for synthetic peptides |
| Solubility | Freely soluble in water | Also soluble in saline |
| Storage temperature | -20 C or below | Protect from repeated freeze-thaw |
| Analytical method | Reverse-phase HPLC | Confirms purity and identity |
| Common synonym | ACTH(4-10) analog | Reflects structural origin |
Quality documentation for research-grade peptide usually includes a certificate of analysis stating purity, identity, and residual counterion content. Batch-to-batch variation in purity and salt form is a recognized issue, and comparisons across suppliers require attention to the exact counterion, for example acetate versus trifluoroacetate. Sequence verification by tandem mass spectrometry provides stronger evidence than a single mass measurement. For any study reporting biological results, the analytical method and the measured purity should be stated explicitly. Independent verification of supplier claims is considered good practice.
Semax is supplied as a lyophilized powder that appears white to off-white. It dissolves readily in water, phosphate-buffered saline, and other aqueous media, which simplifies preparation of working solutions for laboratory use. The nasal products registered in Russia are dilute aqueous solutions, typically around 0.1 percent peptide by weight. Organic solvents are rarely necessary and can complicate handling. Because the peptide is hygroscopic, weighing should be performed quickly and with minimal exposure to ambient humidity.
Solid material is normally kept at minus 20 degrees Celsius in a sealed, desiccated container. Reconstituted solutions are less stable and are usually divided into single-use aliquots before freezing. Repeated freeze-thaw cycles are avoided because they promote aggregation and loss of activity. Light exposure is minimized by using amber glassware or foil wrapping. Published stability data for this peptide are sparse, so recommended storage conditions rest mainly on general practice for short synthetic peptides rather than on dedicated study.
Laboratory descriptions of the material are consistent across suppliers. It appears as a white to off-white lyophilized powder that dissolves readily in water and in polar organic solvents such as dimethyl sulfoxide. Aqueous solutions are clear and colorless at low concentrations. Because the peptide contains methionine, oxidation at the sulfur atom is a recognized degradation pathway, and handling notes usually call for protected, desiccated storage. Reported purity for research-grade lots is generally above 95 percent as measured by reversed-phase high-performance liquid chromatography.
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.
Identity and purity of Semax are established mainly by reversed-phase high-performance liquid chromatography coupled with mass spectrometry. The chromatographic trace gives a purity estimate as a percentage of total peak area, while electrospray or matrix-assisted laser desorption ionization confirms the molecular mass against the calculated value. Amino acid analysis and sequence-specific fragmentation provide further confirmation when a supplier's chain of custody is unclear. Vendors frequently quote a purity figure without stating the detection wavelength or the integration method, which limits how far one number can be compared with another.
Stability depends heavily on physical state. Lyophilized powder held dry, cold and dark retains its content over long periods, whereas dissolved peptide begins to change within days at room temperature. The most cited degradation route is oxidation of the methionine residue, which converts the peptide to a sulfoxide form that elutes differently on chromatography. Hydrolysis of amide bonds and adsorption onto container walls contribute smaller losses. Buffers that exclude oxygen from the headspace slow the oxidation pathway, but no single condition prevents all change indefinitely.
Practical handling follows from those properties. Bulk material is best divided into single-use portions soon after receipt, because each thaw exposes the whole container to moisture and temperature cycling. Vials should be allowed to reach room temperature before opening to prevent condensation on the powder. Low-binding plasticware reduces loss of dilute solutions, and sterile filtration is used when a preparation must remain free of microbial growth. Records of batch number, reconstitution date and storage history are what allow a later analytical result to be interpreted meaningfully.
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.
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.
== Energy consumption == Due to the low temperature, ULT freezers consume high amounts of electric energy and hence are expensive to operate. In 2010, Stanford University had more than 2,000 ULT freezers, which used an estimated 40 billion BTUs of energy and cost the university $5.6 million annually. Newer ULT freezers consume less energy. Nonetheless, a comprehensive report published in 2015 by the Center for Energy Efficient Laboratories (funded by Pacific Gas & Electric, Southern California Edison, and San Diego Gas & Electric utility companies as part of their Emerging Technologies program) found that laboratories in California consumed an estimated 800 GWh/year, with ULT freezers being the greatest contributor to that total. At least as early as 2018, some scientists suggested that laboratories set freezers to –70 °C instead of –80 °C to conserve energy and decrease wear on the freezer's compressor. Depending on the volume of the freezer, the opening frequency of the users as well as the number of samples, the energy consumption starts from ca. 11 kWh/day and higher. The US government calculates 20 kWh/day. A study performed at the University of Edinburgh showed that the New Brunswick U570 HEF model consumed slightly under 10 kWh/day. Without any data, the University of Michigan claimed that "older model" ULT devices could consume "up to 30 kWh/day". A sales pitch written in 2023 quoted "16-22 KWh of electricity per day". To reduce the energy consumption, the insulation should be as efficient as possible.
November 23, 2008: Hawaii Economists at the University of Hawaii reported that the state entered the recession in the previous quarter based on the drop in tourist figures and growing unemployment, with 8,800 jobs expected to be cut in 2009.
Uhthoff's phenomenon, a reversible exacerbation of symptoms following a rise in body temperature, and Lhermitte's sign, an electrical sensation that runs down the back when flexing the neck, are particularly characteristic of MS, although may not always be present. 60–80% of MS patients find that symptoms, such as fatigue, are affected by changes in body temperature. MS may also present with eye movement impairments, such as internuclear ophthalmoplegia or sixth nerve palsy.
Fatty acids are made by fatty acid synthases that polymerize and then reduce acetyl-CoA units. The acyl chains in the fatty acids are extended by a cycle of reactions that add the acyl group, reduce it to an alcohol, dehydrate it to an alkene group and then reduce it again to an alkane group. The enzymes of fatty acid biosynthesis are divided into two groups: in animals and fungi, all these fatty acid synthase reactions are carried out by a single multifunctional type I protein, while in plant plastids and bacteria separate type II enzymes perform each step in the pathway. Terpenes and isoprenoids are a large class of lipids that include the carotenoids and form the largest class of plant natural products. These compounds are made by the assembly and modification of isoprene units donated from the reactive precursors isopentenyl pyrophosphate and dimethylallyl pyrophosphate. These precursors can be made in different ways. In animals and archaea, the mevalonate pathway produces these compounds from acetyl-CoA, while in plants and bacteria the non-mevalonate pathway uses pyruvate and glyceraldehyde 3-phosphate as substrates. One important reaction that uses these activated isoprene donors is sterol biosynthesis. Here, the isoprene units are joined to make squalene and then folded up and formed into a set of rings to make lanosterol. Lanosterol can then be converted into other sterols such as cholesterol and ergosterol.
Sources: en.wikipedia.org
=== External phylogeny === Animals are monophyletic, meaning they are derived from a common ancestor. Animals are the sister group to the choanoflagellates, with which they form the Choanozoa. Ros-Rocher and colleagues (2021) trace the origins of animals to unicellular ancestors, providing the external phylogeny shown in the cladogram. Uncertainty of relationships is indicated with dashed lines. The animal clade had certainly originated by 650 mya, and may have come into being as much as 800 mya, based on molecular clock evidence for different phyla.
== Sequels and prequel == A sequel, titled Underworld: Evolution, in which Marcus fully awakens, was released January 20, 2006. The prequel Underworld: Rise of the Lycans, which gives more detail about the creation of the Lycan species and Lucian's hatred, was released January 23, 2009. A second sequel, Underworld: Awakening, was released on January 20, 2012, and a third sequel, Underworld: Blood Wars, was released on January 6, 2017.
Whole blood and other blood components Organ transplantation and tissue transplants Stem-cell therapy Antibodies for passive immunity (e.g., to treat a virus infection) Human reproductive cells Human breast milk Fecal microbiota Some biologics that were previously extracted from animals, such as insulin, are now more commonly produced by recombinant DNA.
Sources: en.wikipedia.org
It is associated with the melanocortin receptor family, particularly subtypes found in the central nervous system. This interaction is separate from the adrenal pathway activated by full-length ACTH.
Peptidases degrade the compound within minutes in circulation. This short half-life is one reason nasal delivery is used, placing the substance close to the olfactory and trigeminal pathways.
No large multicenter trials have been published in English-language journals. The existing human evidence consists mainly of smaller studies conducted in Russia, which limits generalization.
It is described as a synthetic analogue of the ACTH(4–10) fragment, a short segment of adrenocorticotropic hormone. Its sequence differs from that fragment and includes two proline residues, which influence stability and behaviour in solution.