Everything below concerns heptapeptide. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2025-08-24. Where a claim depends on a specific study, the study is described rather than over-claimed.
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 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.
Pharmacological accounts link semax to melanocortin signalling and to modulation of neurotrophic factor expression, particularly brain-derived neurotrophic factor and nerve growth factor. Much of this evidence comes from rodent studies using intranasal delivery, a route chosen because it allows peptides to reach the central nervous system with limited systemic exposure. Whether the same mechanisms operate in humans at comparable magnitude remains an open question. The precise receptor or receptors responsible for the reported behavioural and neuroprotective effects have not been conclusively identified.
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.
| 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 |
The compound was developed during the 1980s at the Institute of Molecular Genetics in Moscow as part of research on fragments of adrenocorticotropic hormone. Early work examined short ACTH-derived sequences that retained neurotrophic effects while lacking the endocrine activity of the full hormone. Semax entered clinical use in Russia during the 1990s, where it received registration for several neurological indications. Outside that region it remained primarily a laboratory research material rather than an approved therapeutic. English-language literature on it grew more slowly and frequently cited the original Russian studies.
Terminology around the compound varies by source. It appears in catalogues and papers as Semax, as the heptapeptide ACTH(4-7)-Pro-Gly-Pro, and under various alphanumeric laboratory codes used by individual suppliers. These names refer to the same sequence but may imply different salt forms, purity grades, or counter-ions. Peptide databases usually list the free base mass, while product descriptions sometimes report acetate or trifluoroacetate salts with a different formula weight. Because naming conventions for research peptides are not standardised across vendors, checking the declared sequence and measured mass is more reliable than relying on a trade name alone.
Semax is a synthetic heptapeptide with the sequence Met-Glu-His-Phe-Pro-Gly-Pro. Its design combines the ACTH(4-7) core fragment with a C-terminal Pro-Gly-Pro extension, a modification intended to improve stability and prolong activity. The molecule is hydrophilic, carries no lipid chains or glycosylation, and has a theoretical mass just over 810 daltons in its free form. All seven residues are proteinogenic amino acids, so no non-natural building blocks appear in the backbone. A free N-terminal methionine and C-terminal proline define the unmodified parent peptide.
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.
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.
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.
Semax is a synthetic heptapeptide developed in the Soviet Union during the 1980s by researchers at the Institute of Molecular Genetics in Moscow. It was designed as a truncated analog of adrenocorticotropic hormone, retaining only the fragment spanning residues four through ten. Investigators sought a peptide that would preserve the cognitive effects associated with ACTH while eliminating the hormonal stimulation of the adrenal cortex. The compound entered clinical use in Russia during the following decade.
Semax is a synthetic heptapeptide whose sequence is Met-Glu-His-Phe-Pro-Gly-Pro. The first four residues correspond to the ACTH(4-10) fragment, while the terminal Pro-Gly-Pro extension was added to improve metabolic stability. Its molecular formula is C37H51N9O10S and its monoisotopic mass is approximately 813.9 Da. The compound is classified as a peptide research chemical and as a registered pharmaceutical product in Russia, but it does not hold marketing approval in the European Union or the United States. Naming conventions vary across supplier catalogs.
Development of the compound took place in the Soviet Union during the 1980s, largely through peptide research groups affiliated with the Shemyakin-Ovchinnikov Institute and Moscow State University. Investigators screened fragments of adrenocorticotropic hormone for activity on the central nervous system while attempting to separate cognitive effects from hormonal ones. The shortened sequence was selected because it retained behavioral activity in animal models without stimulating corticosteroid release. Early publications described the molecule as an ACTH(4-10) analog.
Published research on this peptide originates mainly from Russian laboratories, and the wider international literature is comparatively thin. Studies have used rodent models of stroke, hypoxia, and memory tasks, with a smaller number of human trials reported. Reported outcomes include changes in attention and memory measures, along with effects on neurotrophic factor expression in some experiments. Small sample sizes, inconsistent dosing protocols, and limited independent replication are widely noted limitations, so the strength of the clinical evidence remains an open question.
Bradbury AF, Finnie MD, Smyth DG (1982). "Mechanism of C-terminal amide formation by pituitary enzymes". Nature. 298 (5875): 686–8. Bibcode:1982Natur.298..686B. doi:10.1038/298686a0. PMID 7099265. S2CID 4324776. Bradbury AF, Smyth DG (1987). "Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid". Eur. J. Biochem. 169 (3): 579–84. doi:10.1111/j.1432-1033.1987.tb13648.x. PMID 3691506. Glembotski CC (1985). "Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules". Arch. Biochem. Biophys. 241 (2): 673–83. doi:10.1016/0003-9861(85)90594-6. PMID 2994573. Katopodis AG, Ping D, May SW (1990). "A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation". Biochemistry. 29 (26): 6115–20. doi:10.1021/bi00478a001. PMID 2207061. Murthy AS, Keutmann HT, Eipper BA (1987). "Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". Mol. Endocrinol. 1 (4): 290–9. doi:10.1210/mend-1-4-290. PMID 3453894. Murthy AS, Mains RE, Eipper BA (1986). "Purification and characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". J. Biol. Chem. 261 (4): 1815–22. doi:10.1016/S0021-9258(17)36013-1. PMID 3944110.
== History == Salad and Go was founded in 2013 in Gilbert, Arizona by Tony and Roushan Christofellis. The co-founders asked Chef Daniel Patino to help them develop the concept. Chef Patino remains an executive chef for the brand. In March 2022, industry veteran Charlie Morrison joined Salad and Go as Chief Executive Officer (CEO). Since Morrison joined, the brand has expanded rapidly into major markets including the Dallas–Fort Worth metroplex, Houston, Las Vegas and Oklahoma City while continuing to open locations in its home state of Arizona. Salad and Go was on track to have a total of 135 stores open by the end of 2023. In January 2024, CEO Charlie Morrison said it was on pace to continue to open up a restaurant a week and described his plans for thousands of locations. On September 19, 2025, Salad and Go closed all stores in Houston, San Antonio, and Austin, along with some in North Texas, with a total of 41 closures. New CEO Mike Tattersfield stated the move was to focus on more disciplined growth. In January 2026, Salad and Go announced it would be closing all its remaining Texas and Oklahoma locations and focusing on strengthening its operations in Arizona and Nevada. The company also announced it would be relocating its headquarters from Coppell, Texas, back to the Phoenix area. On August 4, 2026, Salad and Go filed for Chapter 11 bankruptcy protection and announced the permanent closure of all remaining locations effective the next day, August 5. As a result, plans for the new headquarters were scrapped.
FSH is used commonly in infertility therapy, mainly for ovarian hyperstimulation as part of IVF. In some cases, it is used in ovulation induction for reversal of anovulation as well. FSH is available mixed with LH activity in various menotropins including more purified forms of urinary gonadotropins such as Menopur, as well as without LH activity as recombinant FSH (Gonapure, Gonal F, Follistim, Follitropin alpha).
=== Status epilepticus === Status epilepticus may be defined as seizure activity lasting beyond five minutes and needing anticonvulsant medication. Several guidelines recommend the use of propofol for the treatment of refractory status epilepticus.
production of mRNA molecules (including splicing), initiation of these molecules with help of initiation factors (e.g., the initiation can include the circularization step though it is not universally required), initiation of translation, recruiting the small ribosomal subunit, assembly of full ribosomes, elongation, (i.e. movement of ribosomes along mRNA with production of protein), termination of translation, degradation of mRNA molecules, degradation of proteins. The process of amino acid building to create protein in translation is a subject of various physic models for a long time starting from the first detailed kinetic models such as or others taking into account stochastic aspects of translation and using computer simulations. Many chemical kinetics-based models of protein synthesis have been developed and analyzed in the last four decades. Beyond chemical kinetics, various modeling formalisms such as Totally Asymmetric Simple Exclusion Process, Probabilistic Boolean Networks, Petri Nets and max-plus algebra have been applied to model the detailed kinetics of protein synthesis or some of its stages. A basic model of protein synthesis that takes into account all eight 'elementary' processes has been developed, following the paradigm that "useful models are simple and extendable". The simplest model M0 is represented by the reaction kinetic mechanism (Figure M0). It was generalise to include 40S, 60S and initiation factors (IF) binding (Figure M1'). It was extended further to include effect of microRNA on protein synthesis.
Sources: en.wikipedia.org
Very common (>10% of people with pregabalin): dizziness, drowsiness. Common (1–10% of people with pregabalin): peripheral edema, blurred vision, diplopia, increased appetite and subsequent weight gain, euphoria, confusion, vivid dreams, changes in libido (increase or decrease), irritability, ataxia, attention changes, feeling high, memory impairment, tremor, dysarthria, paresthesia, vertigo, dry mouth, constipation, nausea, vomiting, flatulence, erectile dysfunction, fatigue, feelings of drunkenness, abnormal walking, asthenia, nasopharyngitis, increased creatine kinase level. Infrequent (0.1–1% of people with pregabalin): depression, lethargy, agitation, anorgasmia, hallucinations, myoclonus, hypoaesthesia, hyperaesthesia, tachycardia, hypersalivation, hypoglycemia, excessive sweating, flushing, rash, muscle cramp, myalgia, arthralgia, urinary incontinence, dysuria, thrombocytopenia, kidney calculus. Rare (<0.1% of people with pregabalin): neutropenia, first-degree heart block, hypotension, hypertension, pancreatitis, dysphagia, oliguria, rhabdomyolysis, suicidal thoughts or behavior. Cases of recreational use, with associated adverse effects, have been reported.
=== Transport === Another difference between eukaryotes and prokaryotes is mRNA transport. Because eukaryotic transcription and translation is compartmentally separated, eukaryotic mRNAs must be exported from the nucleus to the cytoplasm—a process that may be regulated by different signaling pathways. Mature mRNAs are recognized by their processed modifications and then exported through the nuclear pore by binding to the cap-binding proteins CBP20 and CBP80, as well as the transcription/export complex (TREX). Multiple mRNA export pathways have been identified in eukaryotes. In spatially complex cells, some mRNAs are transported to particular subcellular destinations. In mature neurons, certain mRNA are transported from the soma to dendrites. One site of mRNA translation is at polyribosomes selectively localized beneath synapses. The mRNA for Arc/Arg3.1 is induced by synaptic activity and localizes selectively near active synapses based on signals generated by NMDA receptors. Other mRNAs also move into dendrites in response to external stimuli, such as β-actin mRNA. For export from the nucleus, actin mRNA associates with ZBP1 and later with 40S subunit. The complex is bound by a motor protein and is transported to the target location (neurite extension) along the cytoskeleton. Eventually ZBP1 is phosphorylated by Src in order for translation to be initiated. In developing neurons, mRNAs are also transported into growing axons and especially growth cones. Many mRNAs are marked with so-called "zip codes", which target their transport to a specific location.
The Montessori Middle School Program completes the Montessori studies for students progressing to the seventh and eighth grades. An interdisciplinary teaching team provides the Montessori Program for multidisciplinary learning to include English Language Arts, mathematics, science and social studies. At the high school level, the student can apply for entry to Biotechnology, Biomedical, Military Academy, Center for the Visual & Performing Arts and/or the Science & Technology Center. Locations:
=== CT Scan === A temporal-bone CT using thin slices makes it possible to diagnose the degree of stenosis and atresia of the external auditory canal, the status of the middle ear cavity, the absent or dysplastic and rudimentary ossicles, or inner ear abnormalities such as a deficient cochlea. Two- and three-dimensional CT reconstructions with VRT and bone and skin-surfacing are helpful for more accurate staging and the three-dimensional planning of mandibular and external ear reconstructive surgery.
Sources: en.wikipedia.org
== Geography == Yavne is a city in the Central District of Israel, located about six kilometers from the Mediterranean Sea in the southern coastal plain region, on the eastern border of the Yavne sand dunes. It is situated between the moshav of Ben Zakai to the south, Ashdod, Gan Yavne, Hazor Ashdod, and Nitzanim to the southwest, Gan Raveh and Kfar HaNagid to the north, Givat Brenner to the east, Bait Gamliel to the southeast, Rehovot to the east-southeast, and Gealya to the northeast.
=== Challenges to implementation === Arsenic removal technologies are traditional treatment processes that have been tailored to improve the removal of arsenic from drinking water. Although some of the removal processes, such as precipitative processes, adsorption processes, ion exchange processes, and separation (membrane) processes, may be technically feasible, their cost may be prohibitive. For underdeveloped countries, the challenge is finding the means to fund such technologies. The Environmental Protection Agency, for example, has estimated the total national annualized cost of treatment, monitoring, reporting, record keeping, and administration to enforce the MCL rule to be approximately $181 million. Most of the cost is due to the installation and operation of the treatment technologies needed to reduce arsenic in public water systems.
Phosphorylation changes the conformation of an enzyme to a more active or inactive way (e.g. regulation of glycogen phosphorylase). Each phosphate group contains two negative charges, so the addition of this group can cause an important change in the conformation of the enzyme. The phosphate can attract positively charged amino acids or create repulsive interactions with negatively charged amino acids. These interactions can change the conformation and the function of the enzyme. When a phosphatase enzyme removes the phosphate groups, this enzyme returns to its initial conformation. Phosphorylation modifies the affinity of the enzyme to the substrate (e.g. phosphorylation of isocitrate dehydrogenase creates electrostatic repulsion which inhibits the union of the substrate to the active center). Phosphorylation can take place in the active center of the enzyme. It can change the conformation of this active center, so it can recognize the substrate or not. Also, the ionized phosphate can attract some parts of the substrate, which can join to the enzyme. Phosphorylation and dephosphorylation may take place as a result of the response to signals that warn about a change in the cell state. This means that some pathways where regulatory enzymes participate are regulated by phosphorylation after a specific signal: a change in the cell. Some enzymes can be phosphorylated in multiple sites.
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 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.