If you have been reading about telomerase 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.
Updated 2025-11-30. Numbers and descriptions here follow the published literature rather than marketing material.
Chemically, the molecule consists of four amino acid residues joined by three peptide bonds, with a free N-terminal amino group and a free C-terminal carboxyl group. Its molecular formula is C14H22N4O9, and its monoisotopic mass is approximately 390 daltons. The acidic glutamate and aspartate side chains give the peptide a net negative charge near neutral pH, a property that shapes its chromatographic behaviour and solubility profile. No disulfide bridges or other post-translational modifications are present, so the primary sequence alone defines the structure.
Most experimental work has been carried out in cell culture and animal models. Several reports describe changes in telomerase activity and proliferation in cultured cells, while rodent studies have examined lifespan, melatonin rhythm and reproductive endpoints. Human data remain limited, and much of the published clinical material consists of small trials with incomplete reporting of methods and controls. Whether the cell and animal findings translate into measurable effects in people is an open question, and the mechanistic basis of the reported telomerase changes is not fully established.
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.
Short peptides such as AEDG are normally supplied as a freeze-dried solid and are kept dry, cold, and shielded from light. Holding at minus twenty degrees Celsius is common for the long term, while a refrigerator suffices for brief periods before use. The material takes up moisture to some degree, so containers should stay sealed and be allowed to reach room temperature before opening, which limits condensation on the contents. Repeated warming and cooling of a single container is discouraged because it admits water and can lower the amount of intact peptide.
Dissolution is usually performed in water or a suitable aqueous buffer, and the resulting liquid is divided into single-use portions before freezing. Freeze-thaw cycling is a recognised source of loss for short peptides, since each cycle can encourage aggregation or adsorption onto container walls. Working solutions are generally kept cold and used within a short window, although published stability data specific to epitalon are thin. Containers should be marked with concentration and date, and solutions examined for cloudiness before use.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Linear tetrapeptide | Four residues joined by three peptide bonds |
| Sequence | Ala-Glu-Asp-Gly | Commonly abbreviated AEDG |
| Molecular formula | C14H22N4O9 | Free acid form |
| Monoisotopic mass | Approximately 390 Da | Matches values reported from mass spectrometry |
| Net charge near neutral pH | Negative | Contributed by glutamate and aspartate side chains |
Epitalon is a synthetic tetrapeptide with the sequence alanine–glutamate–aspartate–glycine, commonly abbreviated AEDG. Its design traces to epithalamin, a peptide fraction prepared from bovine pineal gland extracts that researchers in Saint Petersburg began investigating in the 1970s. The compound has a molecular formula of C14H22N4O9 and a nominal molecular mass near 390 daltons. It holds no approved drug status in the United States or the European Union, and material sold under this name is generally offered as a research chemical rather than a finished pharmaceutical product.
Proposed mechanisms centre on cell-culture observations rather than a defined receptor interaction. Several reports describe increased expression of the telomerase catalytic subunit after exposure of cultured human cells, and the authors attributed the effect to short peptide fragments entering the nucleus and influencing gene transcription. No receptor for the tetrapeptide has been identified, and the free peptide is expected to be degraded rapidly by plasma peptidases. Whether any measurable fraction reaches intact tissues after administration remains an unresolved question rather than an established finding.
The published literature is dominated by a small number of research groups, much of it in Russian-language journals, and independent replication outside those groups is limited. Studies are typically small, use cultured cells or rodent models, and report endpoints that differ between papers, which makes comparison difficult. Large randomised human trials have not appeared in the indexed literature. Questions about absorption, distribution and clearance are therefore still treated as open in reviews that mention the compound.
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.
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.
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.
Material sold for research use varies widely in documented quality. A useful verification package includes a certificate of analysis that states peptide content rather than only net weight, the chromatographic method and column used, and a mass spectrum consistent with the expected mass. Independent testing by a third-party laboratory is occasionally reported. Statements of identity resting only on a supplier label provide little assurance, and the gap between nominal mass and actual peptide content can be substantial once counterions and residual water are counted.
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For four months, as liability issues were resolved, American blepharospasm patients traveled to Canadian eye centers for their injections. Based on data from thousands of people collected by 240 investigators, Oculinum Inc (which was soon acquired by Allergan) received FDA approval in 1989 to market Oculinum for clinical use in the United States to treat adult strabismus (crossed eyes) and blepharospasm (uncontrollable blinking). Allergan then began using the trademark Botox. This original approval was granted under the 1983 US Orphan Drug Act.
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The Cameron Prize for Therapeutics of the University of Edinburgh is awarded by the College of Medicine and Veterinary Medicine to a person who has made any highly important and valuable addition to practical therapeutics in the previous five years. The prize, which may be awarded biennially, was founded in 1878 by Andrew Robertson Cameron of Richmond, New South Wales, with a sum of £2,000. The University's senatus academicus may require the prizewinner to deliver one or more lectures or to publish an account on the addition made to practical therapeutics. A list of recipients of the prize dates back to 1879.
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Sources: en.wikipedia.org
It is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, often abbreviated AEDG. The molecule is linear and contains no modified residues, so it is fully described by its sequence.
The compound came out of work on epithalamin, a peptide preparation derived from pineal tissue, conducted largely in Russian laboratories. Later studies in other countries examined it mainly in cell cultures and animal models.
The tetrapeptide sequence is a synthetic construct rather than a described circulating peptide. It was derived by analogy to peptide fractions obtained from tissue extracts, not isolated from blood or tissue as such.
Reversed-phase high-performance liquid chromatography is run alongside mass spectrometry. The chromatogram separates components and gives a purity figure, while the mass spectrum confirms that the measured molecular mass matches the expected sequence. Neither measurement on its own is treated as sufficient.