This is a working overview of aspartimide, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2025-08-17. Anything still debated is marked as such rather than presented as settled.
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.
The proposed relationship between epitalon and pineal function is a central part of its background. Khavinson's group reported that short peptides corresponding to regions of larger pineal proteins could influence gene expression in cells. Epitalon was framed as a synthetic analogue of an active fragment rather than a direct isolation product. Whether the tetrapeptide reproduces the effects of the parent extract is an open question, because comparative studies are limited and the parent extract itself is not a single defined substance.
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.
The most frequently cited laboratory finding is that AEDG increased telomerase activity and extended telomere length in cultured human somatic cells. That work used fetal fibroblast strains and reported changes in enzyme activity alongside altered division counts. Replication by unrelated groups has been limited, and the published record is largely a single-laboratory series rather than a multi-centre programme. The result supports a hypothesis about peptide influence on gene expression in cell culture; it does not by itself establish an effect on telomere length in living animals or in people.
Animal and clinical reports appear mainly in Russian-language journals from the 1990s and 2000s, covering endpoints such as melatonin rhythm, lifespan in aged rodents, and retinal function. Many of these papers involve small groups, lack blinding or placebo comparison, and are difficult to retrieve through indexed databases. Review articles published in English generally summarise the claims without reanalysing the underlying data. Because no large randomised trial exists, the clinical importance of these reported effects stays unresolved and is properly described as an open question.
| Property | Value | Notes |
|---|---|---|
| Amino acid sequence | Ala-Glu-Asp-Gly | Tetrapeptide, often abbreviated AEDG |
| Molecular formula | C14H22N4O9 | Free peptide, unmodified termini |
| Molecular weight | ~390.35 Da | Calculated for the free acid form |
| Appearance | White to off-white powder | Typical lyophilized product form |
| Solubility class | Freely soluble in water | Two acidic residues dominate ionic character |
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.
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.
Discussions in the literature often conflate three distinct entities: the pineal extract epithalamin, the isolated tetrapeptide AEDG, and commercial preparations sold under similar names. Reviews citing older Russian-language studies sometimes omit detail on purity, route of administration and control groups, which makes cross-study comparison difficult. Researchers working with the compound generally note the need for independent replication, standardized enzyme assays, and clearer reporting of peptide identity. These caveats are relevant when weighing claims that appear in secondary sources rather than in primary reports.
（TG:@pojiaai）Epitalon is a synthetic linear tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. It emerged from work on epithalamin, a peptide fraction prepared from bovine pineal tissue, and was designed as a short, chemically defined analogue of that extract. Early publications came mainly from Russian laboratories studying pineal peptides and aging-related endpoints. The compound appears in the literature under several spellings, including epithalon and epithalone, which complicates systematic searching. Its small size makes solid-phase assembly and routine analytical characterization straightforward.
Reference material is normally supplied as a lyophilised powder in a sealed vial. Product literature typically recommends storage at minus twenty degrees Celsius or colder, protected from light and moisture. Freeze-thaw cycling is usually avoided because repeated condensation can introduce water into the vial. Working solutions are commonly prepared fresh, aliquoted, and kept cold for short periods rather than stored at ambient temperature. Labelling the date of opening helps track how long a vial has been in use.
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.
== Inductively-Couple Plasma/Mass Spectrometry (ICPMS) == In 1983, SCIEX introduced the first commercial ICPMS system for inorganic analysis. Shortly after introduction, a joint venture was formed with Perkin Elmer to market and sell this product. The ICPMS joint venture business was fully acquired by PerkinElmer in 2010.
== General characteristics == Pseudomonas fluorescens has multiple flagella, an extremely versatile metabolism, and can be found in the soil and in water. It is an obligate aerobe, but certain strains are capable of using nitrate instead of oxygen as a final electron acceptor during cellular respiration. Optimal temperatures for growth of P. fluorescens are 25–30°C. It tests positive for the oxidase test, and is also a nonsaccharolytic bacterial species. Heat-stable lipases and proteases are produced by P. fluorescens and other similar pseudomonads. These enzymes cause milk to spoil, by causing bitterness, casein breakdown, and ropiness due to production of slime and coagulation of proteins.
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Sources: en.wikipedia.org
== External links == Carbonate derivatives of 14β-hydroxycodeine "viz., 14β-hydroxy-6-O-(methoxycarbonyl)codeine, 6-O-methoxycarbonyl-14β-(methoxycarbonyloxy)codeine, and 14β-acetoxy-6-O-methoxy-carbonylcodeine, potential substrates for ring C modification in morphinane (sic) alkaloids, were synthesized for the first time." Russian Chemical Bulletin. August 2008, Volume 57, Issue 8, pp 1773–1774. Date: 11 Aug 2009; I. V. Evsikova, S. K. Moiseev, P. V. Petrovskii, V. N. Kalinin. Published in Russian in Izvestiya Akademii Nauk. Seriya Khimicheskaya, No. 8, pp. 1739–1740
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Sources: en.wikipedia.org
Epitalon is a synthetic tetrapeptide composed of four amino acids: alanine, glutamate, aspartate, and glycine. It is written as Ala-Glu-Asp-Gly. The free peptide has a molecular weight of about 390 daltons and is normally supplied as a lyophilized powder.
No. Epitalon is chemically synthesized, not extracted. It was designed as a short synthetic fragment conceptually related to larger pineal peptides studied in the same research tradition, particularly the extract known as epithalamin. The two are distinct materials with different compositions.
The term bioregulator is used in this research tradition for short peptides proposed to influence gene expression or cell function. Epitalon is grouped with other synthetic short peptides under this label. The term reflects a proposed mechanism rather than an established drug classification.
Small studies with human participants have been reported, chiefly in Russian-language journals, but they are limited in size and design. No large randomised controlled trial with published results is available.