Everything below concerns Epitalon. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2026-03-05. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
Identity and purity of epitalon samples are normally established by reversed-phase high-performance liquid chromatography with ultraviolet detection near 214 nanometres, combined with mass spectrometry. The mass spectrum confirms the expected molecular ion and can reveal truncated or oxidised by-products. Amino acid analysis after acid hydrolysis verifies that the four residues are present in the expected ratio. Certificates typically report a purity figure taken from chromatographic peak area, expressed as a percentage of total integrated signal.
Lyophilised epitalon is generally held at minus twenty degrees Celsius in a sealed container kept dry and dark. Cooler conditions are sometimes recommended for long-term archives. The solid takes up moisture readily enough that repeated opening of a vial introduces water, so dividing a batch into smaller portions before storage lowers degradation risk. Aqueous solutions are less durable than the dry powder and are usually prepared shortly before use, then kept cold and shielded from light to slow hydrolysis and oxidation.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Free acid form of the tetrapeptide |
| Molecular mass | About 390.35 Da | Calculated monoisotopic value |
| Appearance | White to off-white powder | Typical lyophilized presentation |
| Solubility | Soluble in water | Also dissolves in buffered saline |
| Storage temperature | Minus 20 degrees Celsius | Dry, dark conditions; avoid repeated thawing |
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.
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.
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.
The parent extract epithalamin was characterised as a low-molecular-weight fraction of pineal tissue rather than a single defined chemical entity. Researchers fractionated it and tested successive fragments for activity, a screening approach typical of peptide discovery work in that era. Epitalon emerged from that process as one of the shorter sequences of interest. Because the original extract was never fully resolved into individual components, claims about which constituent drives a given effect rest on inference. This distinction matters when reading older reports that attribute extract observations to the tetrapeptide itself.
Epitalon is a synthetic tetrapeptide with the residue sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its monoisotopic mass is approximately 390.35 daltons, and it is usually supplied as a lyophilised trifluoroacetate or acetate salt. The compound was derived from a pineal gland extract called epithalamin, a heterogeneous preparation investigated in the former Soviet Union. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology described the tetrapeptide as a constituent fragment of that extract. Commercial material is offered as a laboratory reagent rather than as a finished pharmaceutical product.
Literature searches for this compound must account for several spelling variants. Indexing databases contain epitalon, epithalon, epithalone, and AEDG, and relevant records are scattered across Russian-language and English-language journals that do not consistently cross-cite. Early publications describe the parent extract as a mixture of many peptides, whereas later work addresses the single synthetic tetrapeptide. That shift in nomenclature complicates comparison between studies, because extract data and tetrapeptide data are sometimes cited interchangeably. A search strategy omitting the alternate spellings will return an incomplete set of references.
=== Physiological effects === According to a dose-response study in human subjects, dimethyltryptamine administered intravenously slightly elevated blood pressure, heart rate, pupil diameter, and rectal temperature, in addition to elevating blood concentrations of beta-endorphin, corticotropin, cortisol, and prolactin; growth hormone blood levels rose equally in response to all doses of DMT, and melatonin levels were unaffected."
Narrated by Miriam Margolyes, directed by Karl Sabbagh, made by Skyscraper Productions with KCTS 5 October The Mystery of Anastasia, an Equinox Special, about Anna Anderson; the Romanovs were murdered in Siberia on 17 July 1918; the Forensic Science Service at Aldermaston; forensic scientist William R. Maples; Peter Kurth; David Ellen, of Scotland Yard; Gleb Botkin; Peter Vanezis, Regius Professor of Forensic Medicine (Glasgow) and ears; former Danish ambassador to Germany Herluf Zahle; Ernest Louis, Grand Duke of Hesse hired detective Martin Knopf, who found Anna Anderson's possible name; Geoff Oxley, and facial recognition computing looking at Frances; Patrick Lincoln of London Hospital Medical College, and heredity of blood groups, and the A2 blood group; Peter French, who researched pronunciation; pathologist Hunt MacMillan III and Peter Gill of the Forensic Science Service (Birmingham); in Charlottesville in June 1994; David Enoch (psychiatrist) of the Royal Liverpool University Hospital; the Duke of Edinburgh provided a blood sample to prove mitochondrial DNA, as he was related to Anastasia; Prince Rostislav Rostislavovich Romanov (1938-1999), father of Prince Rostislav Romanov (born 1985); Kevin Sullivan of the Forensic Service; Anna Anderson was not Anastasia, according to mitochondrial DNA of the Duke of Edinburgh.
==== Metabotype informs about treatment outcomes ==== Pharmacometabolomics may be used in a predictive manner to determine the correct course of action in regards to a patient about to undergo some type of drug treatment. This involves determining the metabolic profile of a patient prior to treatment, and correlating metabolic signatures with the outcome of a pharmaceutical treatment course. Analysis of a patient's metabolic profile can reveal factors that may contribute to altered drug metabolism, allowing for predictions of the overall efficacy of a proposed treatment, as well as potential drug toxicity risks that may differ from the general population. This approach has been used to identify novel or previously characterized metabolic biomarkers in patients, which can be used to predict the expected outcome of that patient following treatment with a pharmaceutical compound. One example of the clinical application of pharmacometabolomics are studies that looked to identify a predictive metabolic marker for the treatment of major depressive disorder (MDD)., In a study with antidepressant Sertraline, the Pharmacometabolomics Network illustrated that metabolic profile at baseline of patients with major depression can inform about treatment outcomes. In addition the study illustrated the power of metabolomics for defining response to placebo and compared response to placebo to response to sertraline and showed that several pathways were common to both.
Sources: en.wikipedia.org
"The fibrous variant of Hashimoto's thyroiditis" (1974, with Austin L. Vickery Jr.) "Thymoma in a 12-year-old boy" (1976, with Jane Chatten) "Urinary Ultrastructural Findings in Fabry Disease" (1977, with Patricia J. Lyons) "Examination of Sputum in Legionnaire's Disease" (1978) "Legionnaires' disease: structural characteristics of the organism" (1978, with Philip Nash) "Leydig cell tumors of the testis" (1979, with I. Damjanov and M. A. Jewett) "Ultrastructural Features of Respiratory Cilia in Cystic Fibrosis" (1980, with Douglas S. Holsclaw Jr.) "Postinflammatory pseudotumors of the lung: fibrous histiocytoma and related lesions" (1980, with E. E. Schwartz and G. A. Mandell) "Tolmetin: Association With Reversible Renal Failure and Acute Interstitial Nephritis" (1981, with Ralph Capaldo, Erich A. Everts, and John G. DiGregorio) "Pleomorphism of Legionella pneumophila" (1984, with Shahab Hashemi, Kristy R. Brown, William A. Habib, and Jay M. Hammel) "Cilia in the Human Kidney" (1984, with Joseph J. Morgan) Legionellosis (1985) "Microscopic Nephrocalcinosis in Cystic Fibrosis" (1988, with Leslie J. Krueger and Bonita L. Falkner) "A Self-Limited Febrile Illness Produced in Guinea Pigs Associated With Oral Administration of Legionella pneumophila" (1988, with Jay M. Hammel, Joseph P. Matus, Ronald Poropatich, and Julian Katz) "Diagnostic value of electron microscopy on paraffin-embedded cytologic material" (1993, with Nancy A. Young and Sonya Naryshkin)
In general, polypeptides are unbranched polymers, so their primary structure can often be specified by the sequence of amino acids along their backbone. However, proteins can become cross-linked, most commonly by disulfide bonds, and the primary structure also requires specifying the cross-linking atoms, e.g., specifying the cysteines involved in the protein's disulfide bonds. Other crosslinks include desmosine.
=== Reference biomarkers === Apart from non-destructive sampling, a second area of method development has been the expansion of reference biomarkers. To identify a species using ZooMS, a set of diagnostic biomarkers is used. These biomarkers correspond to particular fragments of the species' collagen protein. The set of known biomarkers at the time of ZooMS' original publication was relatively limited, but recent publications have been expanding this list. A regularly updated list of published biomarkers is maintained by the University of York and can be found here.
Sources: en.wikipedia.org
Epitalon is a synthetic tetrapeptide built from four amino acids: alanine, glutamate, aspartate, and glycine. It is not extracted from a natural source but made in the laboratory by chemical synthesis. Its short length makes it relatively straightforward to produce at high purity.
No naturally occurring free form of the peptide has been described. The four-amino-acid sequence can appear as a fragment within larger proteins, but that is not the same as the intact compound being present as a circulating molecule. Materials used in research are synthetic.
Purity is usually checked by reverse-phase high-performance liquid chromatography, which separates the target peptide from related impurities. Mass spectrometry is commonly used alongside it to confirm molecular mass. Some suppliers also provide amino acid analysis for additional sequence confirmation.
The usual approach is reversed-phase HPLC with ultraviolet detection, reported as a percentage of total peak area. Mass spectrometry is used alongside chromatography to confirm identity rather than purity alone.