A practical reference on AEDG: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
This page was last updated on 2026-03-08 and is reviewed periodically as new material appears.
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.
Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. It was designed at the St. Petersburg Institute of Bioregulation and Gerontology as a short, chemically defined analogue of epithalamin, a fraction obtained from bovine pineal tissue. Small peptide bioregulators of this type formed a long-running line of work there from the 1980s onward. Because the molecule is produced by solid-phase synthesis rather than extraction, its composition is exact and its purity can be measured directly.
The most frequently cited proposed action is induction of telomerase, the enzyme that adds repeat sequences to chromosome ends. Cell-culture work from the originating group reported higher telomerase reverse transcriptase expression and measurable telomere elongation in human somatic cells after exposure. How a four-residue peptide would reach nuclear gene regulation is not established, and no cell-surface receptor or uptake route has been identified. Additional reports describe changes in melatonin secretion, antioxidant enzyme activity and lipid peroxidation in aged animals, but these findings remain mechanistically unconnected to the telomerase observation.
Published evidence comes mainly from Russian-language journals and from a single research group, with small sample sizes and limited independent replication. A few laboratories outside that group have examined related peptides and reported weaker or absent telomerase effects, so the central claim is best described as contested rather than settled. Rodent studies report modest changes in some ageing markers and in survival, but designs vary and control conditions are often sparse. No large randomised trial in humans has been published, and long-term safety data in healthy populations are correspondingly thin.
| Property | Value | Notes |
|---|---|---|
| Identity confirmation | Electrospray or MALDI mass spectrometry | Observed mass compared with theoretical 390.35 Da |
| Purity specification | 95 percent or greater by RP-HPLC | Common convention for research-grade peptide |
| Counter-ion | Acetate or trifluoroacetate | Affects net peptide content of a weighed sample |
| Solution storage | −80 °C as single-use aliquots | Repeated freeze–thaw cycles accelerate loss |
| Main degradation route | Aspartimide formation at Asp-Gly | Produces isoaspartate and related species |
Stability of the tetrapeptide follows ordinary peptide chemistry rather than any unusual structural feature. The aspartate-glycine pair is prone to aspartimide formation under mildly basic or neutral conditions, and deamidation can follow, altering both mass and chromatographic retention. Dry lyophilised powder kept at or below minus twenty degrees Celsius is the usual handling recommendation, with repeated freeze-thaw cycles avoided. Once dissolved in neutral aqueous buffer, degradation proceeds over days to weeks depending on pH and temperature, while acidic conditions generally slow the aspartimide route. A formal stability-indicating study has not been published in the indexed literature.
Because epitalon has no pharmacopoeial monograph, quality assessment depends on supplier documentation and independent testing. Certificates of analysis typically report a purity figure from a single chromatographic run, a measured mass and sometimes an appearance description, but methods and acceptance criteria are not harmonised across vendors. Third-party laboratories can repeat identity and purity measurements, and mismatches between labelled and measured peptide content have been described for research peptides generally. What constitutes adequate identity confirmation for a molecule of this size stays an open question, since mass agreement alone does not separate closely related sequences.
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.
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.
Typical storage for the lyophilized powder is −20 °C or lower, in a sealed container protected from light and moisture. Hygroscopic material should be allowed to equilibrate to room temperature before the vial is opened, which limits condensation on the contents. Working solutions are commonly divided into single-use aliquots and frozen to avoid repeated freeze-thaw cycles. Dilute solutions are more prone to adsorption onto plastic surfaces and to loss during filtration, so procedures that minimize transfers and use low-binding labware are preferable.
Reversed-phase high-performance liquid chromatography is the standard approach for assessing purity, usually with ultraviolet detection near 214 nm, where the peptide bond absorbs. Mass spectrometry, most often with electrospray ionization, confirms the molecular mass and helps reveal truncation or deletion byproducts. Amino acid analysis can verify composition, and counterion content is sometimes measured because peptides purified with trifluoroacetic acid retain variable amounts of that salt. Purity figures reported without a stated method and detection wavelength are difficult to interpret.
Published work on this compound consists mainly of in vitro experiments, animal studies, and small clinical investigations, a substantial share of which appeared in Russian-language journals. Sample sizes are generally small, control conditions differ between studies, and several endpoints rely on markers whose clinical meaning is itself debated. Reviews of the longevity field treat the peptide as an early example of telomerase-directed research rather than an established intervention. Regulatory treatment varies by country: some jurisdictions place it under prescription controls, others treat it as a laboratory material, and importation may be restricted regardless of local status.
Epitalon is a synthetic tetrapeptide whose sequence is alanine–glutamate–aspartate–glycine, commonly abbreviated AEDG. It was developed in Russia during the 1980s and 1990s by investigators associated with the St. Petersburg Institute of Bioregulation and Gerontology, who studied short peptides as regulators of gene expression and tissue function. The alternative spelling epithalon appears interchangeably in the literature, and the two names refer to the same molecule. Outside Russia it is encountered chiefly as a research chemical rather than a licensed medicine, and it holds no approval from the United States Food and Drug Administration or the European Medicines Agency.
The peptide is a synthetic analogue of epithalamin, a preparation extracted from bovine pineal glands. Investigators sought a short, chemically defined molecule that would reproduce some of the endocrine and gerontological observations attributed to the glandular extract. Proposed mechanisms centre on induction of telomerase activity, an effect reported in cultured human somatic cells in the early 2000s, together with influences on melatonin secretion and neuroendocrine regulation. Those mechanisms remain incompletely characterised, and the reported telomerase response has not been consistently reproduced by independent groups working in comparable systems.
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In the drug discovery process of a 5-HT2C agonist, a pharmacophore module has been used to discover novel 5-HT2C receptor ligands. The pharmacophore has four features; one aromatic ring, two hydrophobic features and one positive ionizable feature. Figure 4 shows an example of a compound that fits the agonist pharmacophore perfectly. The nitrogen atom of piperazine fits the positive ionizable feature, the benzofuran part fits the aromatic ring and one hydrophobic, and the trifluoromethane part fits another hydrophobic feature of the pharmacophore.
Sources: en.wikipedia.org
===== MeSH D08.811.682.657 – oxidoreductases acting on aldehyde or oxo group donors ===== MeSH D08.811.682.657.163 – aldehyde oxidoreductases MeSH D08.811.682.657.163.249 – aldehyde dehydrogenase MeSH D08.811.682.657.163.249.750 – omega-crystallins MeSH D08.811.682.657.163.311 – aldehyde oxidase MeSH D08.811.682.657.163.342 – aminomuconate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.374 – aspartate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.468 – benzaldehyde dehydrogenase (NADP+) MeSH D08.811.682.657.163.515 – betaine-aldehyde dehydrogenase MeSH D08.811.682.657.163.562 – glutamate-5-semialdehyde dehydrogenase MeSH D08.811.682.657.163.750 – glyceraldehyde-3-phosphate dehydrogenases MeSH D08.811.682.657.163.750.250 – glyceraldehyde 3-phosphate dehydrogenase (nadp+) MeSH D08.811.682.657.163.750.300 – glyceraldehyde-3-phosphate dehydrogenase (nadp+)(phosphorylating) MeSH D08.811.682.657.163.750.350 – glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) MeSH D08.811.682.657.163.781 – glycolaldehyde dehydrogenase MeSH D08.811.682.657.163.796 – l-aminoadipate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.812 – malonate-semialdehyde dehydrogenase (acetylating) MeSH D08.811.682.657.163.827 – methylmalonate-semialdehyde dehydrogenase (acylating) MeSH D08.811.682.657.163.835 – retinal dehydrogenase MeSH D08.811.682.657.163.843 – succinate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.875 – succinate-semialdehyde dehydrogenase (NAD(P)+) MeSH D08.811.682.657.180 – formate dehydrogenases MeSH D08.811.682.657.350 – ketone oxidoreductases MeSH D08.811.682.657.350.750 – ketoglutarate dehydrogenase complex MeSH D08.811.682.657.350.750.500 – dihydrolipoamide dehydrogenase MeSH D08.811.682.657.350.760 – 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) MeSH D08.811.682.657.350.825 – 2-oxoisovalerate dehydrogenase (acylating) MeSH D08.811.682.657.350.875 – pyruvate dehydrogenase (lipoamide) MeSH D08.811.682.657.350.937 – pyruvate oxidase MeSH D08.811.682.657.350.968 – pyruvate synthase
== Background == The Government of India and UNESCO signed a Memorandum of Understanding (MoU) on 14 July 2006 to establish RCB. The centre is now recognized as a "Category II Centre" by "the principles and guidelines for the establishment and functioning of UNESCO Institutes and Centres". Following approval from the Union Cabinet, the centre became operational from its interim campus at Gurgaon, Haryana from 20 April 2009.
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Sources: en.wikipedia.org
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.
Yes. Trifluoroacetate and acetate ions remain associated with the peptide after purification, so a weighed quantity of powder contains less peptide than the nominal mass suggests. Certificates that report net peptide content rather than raw weight are more directly comparable between suppliers.
Dilute aqueous solutions are less stable than the dry powder and are usually aliquoted and frozen to avoid repeated freeze–thaw cycles. Lyophilised material is best stored desiccated at −20 °C, protected from light. Working solutions are typically prepared fresh from a frozen aliquot.
No. Epithalamin is a peptide-containing extract of bovine pineal glands, while epitalon is a single synthetic tetrapeptide. The extract contains many peptides and other tissue components, so its composition varies between batches in ways that a synthesised sequence does not.