If you have been reading about aspartimide and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Last reviewed on 2026-08-01. Where a claim depends on a specific study, the study is described rather than over-claimed.
The peptide emerged from research carried out in Saint Petersburg from the late 1980s onward, where investigators searched for shorter active fragments of a pineal preparation known as epithalamin. The name epitalon was chosen to reflect that parent extract. Early reports described effects on neuroendocrine markers and on the lifespan of laboratory animals. Much of that work appeared in Russian-language journals, with English translations following later, which affects how readily the original protocols can be assessed by outside groups.
Published studies on epitalon are dominated by a small number of research groups, and independent replication in other laboratories remains limited. Proposed mechanisms include activation of telomerase and modulation of melatonin rhythms, but the evidence for either rests mainly on cell cultures and animal models. Whether the peptide produces comparable effects in humans is an open question, and the absence of large controlled trials means the literature is best read as exploratory rather than settled.
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9, and its calculated molar mass is approximately 390.35 grams per mole. The compound is a short fragment related to a peptide fraction isolated from bovine pineal gland extracts, and it is normally supplied as a lyophilised powder intended for laboratory research. It is not a registered pharmaceutical product in most countries.
Verification of a sample usually begins with reversed-phase high-performance liquid chromatography, which resolves the peptide from truncated sequences and other impurities and expresses purity as a percentage of total peak area. Mass spectrometry by electrospray ionisation or matrix-assisted laser desorption supplies an independent check, because the measured mass can be compared against the theoretical value for AEDG. Amino acid analysis or tandem mass spectrometry sequencing can confirm residue order. Each of these methods answers a different question: a purity figure does not establish identity, and an identity match does not establish how much of the material is intact peptide.
The molecule is a short, linear, hydrophilic peptide that dissolves readily in water or aqueous buffer. Its principal chemical liabilities are hydrolytic rather than oxidative, since it contains no cysteine, methionine, or tryptophan residues. The aspartate–glycine step is a recognised site for aspartimide formation under mildly acidic or basic conditions, generating isoaspartate and succinimide-related products over time. Desiccated lyophilised powder held at −20 °C is comparatively stable, whereas dilute solutions degrade faster and are best frozen as single-use aliquots rather than thawed repeatedly.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Derived from the four-residue sequence |
| Molar mass | About 390.35 g/mol | Free peptide, counter-ion not included |
| Appearance | White to off-white powder | Lyophilised solid from aqueous solution |
| Water solubility | Freely soluble | Short, polar peptide chain |
| Common synonyms | AEDG; epithalone | Catalogues use the names interchangeably |
Interest in epitalon is usually discussed within the broader field of short peptide bioregulators, a category that includes other synthetic di-, tri-, and tetrapeptides studied by the same research group. These compounds share a common rationale: that small fragments of tissue-derived proteins can retain biological activity and can be produced reproducibly. The category as a whole remains outside mainstream pharmacological consensus, and epitalon specifically has a limited presence in independent, non-Russian research literature, which shapes how its evidence base is described.
Epitalon is a synthetic tetrapeptide with the amino acid sequence alanine-glutamate-aspartate-glycine, abbreviated Ala-Glu-Asp-Gly or AEDG. It was developed by the Russian researcher Vladimir Khavinson and colleagues during work on peptide bioregulators derived from the pineal gland. The compound is short enough to be produced by standard solid-phase peptide synthesis and is typically handled as a lyophilized white powder. Its small size distinguishes it from larger pineal peptides such as epithalamin, a complex extract from which the tetrapeptide was conceptually derived.
The four residues give epitalon a molecular formula of C14H22N4O9 and a molecular weight near 390.35 daltons. The presence of two acidic residues, glutamate and aspartate, makes the free peptide strongly acidic, while the alanine and glycine ends provide neutral, nonpolar character. This combination produces a molecule with substantial water solubility. Because there are no cysteine, methionine, or tryptophan residues, the peptide lacks the most common oxidation-sensitive side chains, which simplifies handling compared with many longer peptides.
Solubility is high in water, phosphate-buffered saline and normal saline, a pattern that follows from the two acidic residues in the chain. The peptide dissolves poorly in non-polar solvents such as hexane or chloroform. Stock solutions are often prepared in water first and then diluted into the buffer of interest. Because the molecule is small and hydrophilic, filtration through a low-protein-binding membrane is usually straightforward, and visible particulates are uncommon in freshly made solutions.
Identity and purity are established with reversed-phase high-performance liquid chromatography and mass spectrometry. The chromatogram shows the main peak and any truncated or oxidised by-products, while the mass spectrum confirms the expected 390 dalton mass. Amino acid analysis can corroborate composition when a sample's origin is uncertain. Counterion content, particularly residual trifluoroacetate from purification, is frequently reported alongside purity because it shifts the net mass of the solid.
Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and its calculated monoisotopic mass is approximately 390.35 daltons. The compound does not occur naturally as a free peptide; it is produced by solid-phase peptide synthesis. Because it contains two acidic residues and no basic residues, the neutral form carries a net negative charge at physiological pH. This charge profile influences how the peptide behaves in solution and during chromatographic analysis.
Laboratory-grade epitalon is typically supplied as a lyophilized powder. Purity is commonly assessed with reverse-phase high-performance liquid chromatography, often paired with mass spectrometry to confirm molecular identity. Amino acid analysis and peptide mapping can provide additional confirmation of sequence. Certificates of analysis for research materials frequently report purity above 95 percent, although the methods behind such figures vary between suppliers. The absence of a pharmacopeial monograph means that no single standardized assay defines the compound, so reported results depend on the analytical protocol chosen.
Storage recommendations center on limiting moisture, heat, and light. The dry powder is generally kept at minus 20 degrees Celsius, and some suppliers recommend minus 80 degrees for long-term archival. Once dissolved, solutions are usually aliquoted and frozen to avoid repeated freeze-thaw cycles, which can promote aggregation or degradation. Aqueous stability depends on pH and concentration, and buffered saline is often preferred over plain water for biological work. Stability data specific to epitalon remain limited, so general peptide-handling practices are applied by analogy rather than from product-specific validation.
Laboratory handling begins with dissolution of the lyophilized powder in water or a suitable aqueous buffer. The dry solid is the more stable form, so stock solutions are generally prepared only when required and kept cold afterwards. Repeated freezing and thawing of a solution is avoided because it encourages aggregation and gradual loss of the intact chain. Diluents and containers are selected to limit adsorption of a short peptide onto plastic surfaces and to reduce microbial growth in aqueous preparations.
Stability depends strongly on pH, temperature and the presence of oxygen and trace metals. Cleavage of the backbone proceeds faster under neutral to alkaline conditions, whereas acidic solutions tend to slow that reaction. The aspartate and glutamate side chains can undergo deamidation or imide formation over time, generating closely related impurities. Published stability data specific to epitalon are sparse, so the usable life of a given solution is best regarded as an open question that depends on buffer composition, concentration and storage temperature.
Identity and purity are usually assessed by reversed-phase high-performance liquid chromatography with ultraviolet detection, frequently near 214 nanometers where the peptide bond absorbs. Mass spectrometry, most often with electrospray ionization, confirms the observed molecular mass and helps separate the intact peptide from truncated or modified forms. Amino acid analysis or tandem mass spectrometry can establish residue order. Purity is commonly quoted as an area percentage, yet such values are method-dependent, and comparisons between laboratories require matching column, gradient and detection wavelength.
=== Pharmacokinetics === Due to poor oral absorption, teicoplanin requires intravenous or intramuscular administration for systemic effect. Intramuscular administration achieves approximately 90% bioavailability. The drug exhibits high protein binding (90-95%) and is primarily eliminated through the kidneys unchanged, with minimal liver metabolism (2-3%) via hydroxylation. Clearance is reduced in patients with kidney impairment and is not significantly removed by hemodialysis. Teicoplanin exhibits a long half-life of 45-70 hours, allowing for once-daily dosing after loading doses. Although teicoplanin is primarily approved for intravenous and intramuscular use, several clinical and pharmacokinetic studies have explored its administration via the subcutaneous route. Subcutaneous teicoplanin has been reported as a feasible alternative in selected patients, particularly in outpatient, frail, or palliative care settings. Available evidence suggests that subcutaneous administration achieves pharmacokinetic and pharmacodynamic exposures comparable to intravenous dosing after appropriate loading, with good local tolerability. However, this route of administration remains off-label.
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Amino acids comprise peptides as residues. Peptides are usually linear polymers with a free amine at one end (the so-called N-terminus) and a carboxyl group at the other (the C-terminus). Macrocyclic peptides are a distinct class.
Regarding the significant increases detected, it is worthwhile to consider that the number of pharmaceuticals dispensed for legitimate therapeutic uses may be increasing over time, and DAWN estimates are not adjusted to take such increases into account. Nor do DAWN estimates take into account the increases in the population or ED use between 2004 and 2006. Those at particularly high risk for misuse and dependence are people with a history of alcoholism or drug abuse and/or dependence and people with borderline personality disorder. The poly-drug use of powerful depressant drugs poses the highest level of health concerns due to a significant increase in the likelihood of experiencing an overdose, which may cause fatal respiratory depression. A 1990 study found that diazepam has a higher misuse potential relative to many other benzodiazepines and that some data suggest that alprazolam and lorazepam resemble diazepam in this respect. Anecdotally, injection of alprazolam has been reported, causing dangerous damage to blood vessels, closure of blood vessels (embolization), and decay of muscle tissue (rhabdomyolysis). Alprazolam is not very soluble in water; when crushed in water, it does not fully dissolve (40 μg/ml of H2O at pH 7). There are also reports of alprazolam being snorted. Due to the low weight of a dose, alprazolam, in one case, was distributed on blotter paper in a manner similar to LSD. Misuse of alprazolam and other benzodiazepines has been shown to cause cognitive impairment.
Sources: en.wikipedia.org
=== Role in muscle regeneration === The first step to understanding the importance of macrophages in muscle repair, growth, and regeneration is that there are two "waves" of macrophages with the onset of damageable muscle use– subpopulations that do and do not directly have an influence on repairing muscle. The initial wave is a phagocytic population that comes along during periods of increased muscle use that are sufficient to cause muscle membrane lysis and membrane inflammation, which can enter and degrade the contents of injured muscle fibers. These early-invading, phagocytic macrophages reach their highest concentration about 24 hours following the onset of some form of muscle cell injury or reloading. Their concentration rapidly declines after 48 hours. The second group is the non-phagocytic types that are distributed near regenerative fibers. These peak between two and four days and remain elevated for several days while muscle tissue is rebuilding. The first subpopulation has no direct benefit to repairing muscle, while the second non-phagocytic group does. It is thought that macrophages release soluble substances that influence the proliferation, differentiation, growth, repair, and regeneration of muscle, but at this time the factor that is produced to mediate these effects is unknown. It is known that macrophages' involvement in promoting tissue repair is not muscle specific; they accumulate in numerous tissues during the healing process phase following injury.
== Treatment == There is no known cure for Becker muscular dystrophy yet. Treatment is aimed at control of symptoms to maximize the quality of life which can be measured by specific questionnaires. Activity is encouraged and can be considered vital for long-term survivability for these patients. Inactivity (such as bed rest) or sitting down for too long can worsen the muscle disease. Physical therapy may be helpful to maintain muscle strength. Orthopedic appliances such as braces and wheelchairs may improve mobility and self-care. Immunosuppressant steroids have been known to help slow the progression of Becker muscular dystrophy. The drug prednisone contributes to increased production of the protein utrophin which closely resembles dystrophin, the protein that is defective in BMD. The cardiac problems that occur with EDMD and myotonic muscular dystrophy may require a pacemaker. Other cardiomyopathies seen in Becker muscular dystrophy can also be treated with ACE inhibitors, cardiac transplant, and other personalized treatments. The investigational drug Debio-025 is a known inhibitor of the protein cyclophilin D, which regulates the swelling of mitochondria in response to cellular injury. Researchers decided to test the drug in mice engineered to carry MD after earlier laboratory tests showed deleting a gene that encodes cyclophilin D reduced swelling and reversed or prevented the disease's muscle-damaging characteristics. According to a review by Bushby, et al.
Strychnine poisoning in animals usually occurs from ingestion of baits designed for use against gophers, rats, squirrels, moles, chipmunks and coyotes. Strychnine is also used as a rodenticide, but is not specific to such unwanted pests and may kill other small animals. In the United States, most baits containing strychnine have been replaced with zinc phosphide baits since 1990. In the European Union, rodenticides with strychnine have been forbidden since 2006. Some animals are immune to strychnine; usually these have evolved resistance to poisonous strychnos alkaloids in the fruit they eat, such as fruit bats. The drugstore beetle has a symbiotic gut yeast that allows it to digest pure strychnine. Strychnine toxicity in rats is dependent on sex. It is more toxic to females than to males when administered via subcutaneous injection or intraperitoneal injection. Differences are due to higher rates of metabolism by male rat liver microsomes. Dogs and cats are more susceptible among domestic animals, pigs are believed to be as susceptible as dogs, and horses are able to tolerate relatively large amounts of strychnine. Birds affected by strychnine poisoning exhibit wing droop, salivation, tremors, muscle tenseness, and convulsions. Death occurs as a result of respiratory arrest. The clinical signs of strychnine poisoning relate to its effects on the central nervous system. The first clinical signs of poisoning include nervousness, restlessness, twitching of the muscles, and stiffness of the neck.
Sources: en.wikipedia.org
It is a synthetic tetrapeptide built from alanine, glutamate, aspartate and glycine. The four residues are joined by standard peptide bonds, giving a linear chain rather than a branched structure.
The name derives from epithalamin, a pineal gland extract studied in the former Soviet Union. Researchers proposed that short fragments of that extract carried the biological activity of interest.
No major regulatory agency has approved it as a medicine. It is handled as a research chemical, and products sold under this name are not standardised drugs with defined clinical labelling.
Mass spectrometry provides the identity check, because the observed mass is compared with the theoretical mass of the AEDG sequence. Chromatography separates and quantifies impurities but does not by itself prove which peptide is present. The two techniques are normally used together.