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 2026-01-20 and is reviewed periodically as new material appears.
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.
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.
Material supplied for laboratory use is normally a lyophilised white to off-white powder that dissolves readily in water and in isotonic saline. Lyophilised cakes are hygroscopic and should be equilibrated to room temperature before opening to limit condensation on the solid. Solutions are typically prepared at milligram-per-millilitre concentrations and divided into single-use aliquots, because repeated freeze–thaw cycles degrade short peptides. Aqueous solutions are far less stable than the dry powder, and identity is usually verified by mass spectrometry alongside purity estimation from reversed-phase high-performance liquid chromatography.
Epitalon is a synthetic linear tetrapeptide with the sequence alanine–glutamate–aspartate–glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and the calculated mass is approximately 390.35 g/mol. The compound is made by solid-phase peptide synthesis rather than extracted from tissue, although early work described it as a short fragment of a peptide fraction obtained from bovine pineal extract. In the research literature the spelling epitalon and the variant epithalone both appear, while AEDG is the standard code used in peptide nomenclature.
| Property | Value | Notes |
|---|---|---|
| Peptide sequence | Ala-Glu-Asp-Gly | Often abbreviated AEDG in research literature |
| Common synonyms | Epithalon, epitalon, AEDG | Spelling variants refer to the same tetrapeptide |
| Molecular formula | C14H22N4O9 | Theoretical monoisotopic mass near 390.35 Da |
| Appearance | White to off-white powder | Typically supplied as a lyophilised solid |
| Solubility class | Freely soluble in water | Hydrophilic peptide; dissolves in aqueous buffer |
The compound is described in the literature as a derivative of epithalamin, a preparation obtained from bovine pineal tissue. Work on this peptide family was carried out mainly by a research group in Saint Petersburg beginning in the 1980s, and the substance was later registered for clinical use in Russia under the name Epitalon. Outside that region it is generally treated as a research chemical rather than an approved medicine. Statements about its biological activity rest on a relatively small number of studies, and independent replication remains limited.
In its supplied form epitalon is a white to off-white powder, usually lyophilized and often hygroscopic. It dissolves readily in water and in aqueous buffers, and it is commonly handled as the acetate or trifluoroacetate salt to improve stability during purification and drying. The amide backbone is labile in aqueous media, so solutions are less durable than the dry solid. Handling notes in the chemical literature therefore emphasize keeping the powder dry, cool and shielded from light until it is dissolved.
Residue composition is the property that most cleanly separates verified material from mislabelled samples. Alanine, glutamate, aspartate and glycine appear in that order from the N-terminus, and the two acidic residues sit in the middle of the chain. Because the peptide is short, it can be produced by solid-phase synthesis and characterised by mass spectrometry without ambiguity. Any reported sample whose measured mass departs substantially from 390 daltons is a different compound or a degraded mixture rather than epitalon.
Epitalon is a synthetic tetrapeptide whose four residues are alanine, glutamate, aspartate and glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9 and its monoisotopic mass is near 390.35 daltons. The peptide carries two acidic side chains, so it is neutral to negatively charged in most aqueous buffers. Published reference summaries usually list it under both spellings, epitalon and epithalon, and treat the two names as the same material.
== Literatur == Sven P. Thoms: Ursprung des Lebens. Fischer, Frankfurt 2005, ISBN 3-596-16128-2. Jon R. Lorsch, Jack W. Szostak: In vitro evolution of new ribozymes with polynucleotide kinase activity. In: Nature, Band 371, Nr. 6492, 1. September 1994, S. 31–36; doi:10.1038/371031a0, PMID 7521014 (englisch). Thomas R. Cech, Olke C. Uhlenbeck: Hammerhead nailed down. In: Nature, Band 372, Nr. 6501, 3. November 1994, S. 39–40, doi:10.1038/372039a0 (englisch). B. Alberts, A. Johnson, J. Lewis, M. Raff, K. Roberts, P. Walter: Molekularbiologie der Zelle. 4. Auflage, Wiley-VCH, Weinheim 2004, ISBN 3-527-30492-4. Adam Roth, Zasha Weinberg u. a.: A widespread self-cleaving ribozyme class is revealed by bioinformatics. In: Nature Chemical Biology. 10, 2013, S. 56–60, doi:10.1038/nchembio.1386 (englisch). Nikolaos Papastavrou, David P. Horning, Gerald F. Joyce: RNA-catalyzed evolution of catalytic RNA. In: PNAS, Band 121, Nr. 11, 4. März 2024, S. e23215921; doi:10.1073/pnas.2321592121 (englisch). Dazu: Claudia Krapp: Neuer Einblick in die „RNA-Welt“. Wie sich RNA-Enzyme auf der Urerde evolutionär optimieren konnten. Auf: scinexx.de vom 5. März 2024. Unlocking the Secrets of Life With RNA’s Ancient Code. Auf: SciTechDaily vom 1. April 2024. Quelle: Salk Institute. Edoardo Gianni, Samantha L.-Y. Kwok, Christopher J.-K. Wan, Kevin Goeij, Bryce E. Clifton, Enrico S. Colizzi, James Attwater, Philipp Holliger: A small polymerase ribozyme that can synthesize itself and its complementary strand. In: Science, Band 391, Nr. 6789, 12, Februar 2026, S.
1022–1028; doi:10.1126/science.adt2760, PMC 7618777 (freier Volltext), PMID 41678588 (englisch). Thema: das autokatalytische kurze Polymerase-Ribozym QT45 (Länge: 45 nt). Dazu: Edoardo Gianni, Samantha L. Y. Kwok, Christopher J. K. Wan, Kevin Goeij, Bryce E. Clifton, Enrico S. Colizzi, James Attwater, Philipp Holliger: A small polymerase ribozyme that can synthesize itself and its complementary strand. In: Science, band 391, Nr. 6789, 12. Februar 2026, S. 1022–1028; doi:10.1126/science.adt2760 (englisch). Dazu: Robert Czepel: Urzeugung: Möglicher Urkeim des Lebens entdeckt. Auf: orf.at vom 12. März 2026. Jana Kizina, Almud Lonsing, Jens Harder: Mobile intron RNA from a bacterial predator accumulates in dead archaeal cells. In: Scientific Reports, Band 16, Nr. 14654, 7. Mai 2026; doi:10.1038/s41598-026-51721-6 (englisch). Dazu: Auf frischer Tat ertappt: Ein Gen springt ins Leere. Auf: EurekAlert! vom 18. Juni 2026.
Separase, auch Separin genannt, ist eine Cysteinprotease und spielt eine entscheidende Rolle bei der Regulation mitotischer und meiotischer Vorgänge. Separase leitet die Anaphase durch die Hydrolyse von Cohesin, eines Proteins, welches für die Bindung der Schwesterchromatiden während der frühen Anaphase verantwortlich ist, ein. Beim Menschen wird das Protein Separase durch das Gen ESPL1 (Extra Spindle Pole Bodies Like 1) codiert. Die feste Bindung der Schwesterchromatiden vor der Anaphase sowie ihre rechtzeitige Trennung während der Anaphase sind entscheidend für die Zellteilung und die ordentliche Vererbung. In Säugetieren erfolgt die Schwesterchromatidentrennung in zwei Schritten nach einem klaren Mechanismus. Im ersten Schritt erfolgt die Phosphorylierung von STAG1 und STAG2 im Cohesin-Komplex, anschließend wird im zweiten Schritt die Cohesin Untereinheit SCC1 (RAD21) durch die Separase gespalten, was die endgültige Trennung der Schwesterchromatide einleitet. In S. cerevisiae (Hefe) wird die Separase ebenfalls durch das Gen ESPL1 codiert und durch das Securin Pds1 reguliert. Die beiden Schwesterchromatiden sind initial durch den Cohesin-Komplex miteinander verbunden, bis die Anaphase eingeleitet wird. An diesem Punkt des Zellzyklus werden die Schwesterchromatiden von der mitotischen Spindel auseinandergezogen, sodass letztlich jede entstehende Tochterzelle eines der Schwesterchromatide enthält. Befindet sich eine Zelle nicht in der Teilungsphase, wird Separase an der Spaltung von Cohesin durch die Assoziation mit einem anderen Protein, dem Securin, gehindert.
Genauso verhindert die Phosphorylierung der Separase durch den Cyclin-CDK-Komplex eine unerwünschte bzw. außerplanmäßige Spaltung des Cohesins. So wird auf zwei unterschiedlichen Wegen verhindert, dass Cohesin gespaltet wird und die Schwesterchromatide sich frühzeitig trennen. Anzumerken sei, dass Separase in den meisten Organismen nicht wirksam ist, bevor nicht initial die Bildung eines Separase-Securin Komplexes erfolgt. Das kommt daher, dass Securin bei der Faltung der funktionellen Konformation des Enzyms Separase hilft. Bei der Hefe scheint die Bildung dieses Komplexes jedoch nicht für die funktionelle Konformation der Separase notwendig zu sein, da die Anaphase auch ohne das Vorhandensein von Securin (Securin Deletion) eingeleitet und durchlaufen wird. Die zweite wichtige Funktion der Separase ist die Zentriolentrennung während der Anaphase. Diese Trennung erlaubt die Verdopplung der Zentrosomen im nächsten Zellzyklus.
Sources: de.wikipedia.org
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine–glutamate–aspartate–glycine, also written AEDG. It was developed in Russian gerontology research and is studied for proposed effects on telomerase, melatonin regulation, and neuroendocrine function. It is not an approved pharmaceutical in the United States or the European Union.
No. Epithalamin is a peptide-rich extract prepared from bovine pineal glands, while epitalon is a short synthetic peptide designed as a defined analogue of it. The synthetic version was intended to provide a reproducible molecule with some of the same proposed biological activity.
Telomere elongation and telomerase activation have been reported in cultured human somatic cells, but evidence from living human subjects is limited and has not been independently confirmed at scale. Reported findings come largely from small studies with differing designs, so the question remains open rather than settled.
It is a synthetic tetrapeptide. Its sequence was derived from research on peptide fractions of bovine pineal extract, and the intact AEDG sequence has not been demonstrated as an abundant free peptide in human tissue.