AEDG raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
Reviewed 2025-10-15. Anything still debated is marked as such rather than presented as settled.
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.
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 the common name for a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, usually abbreviated AEDG. All four residues are proteinogenic amino acids, and the free peptide has a calculated mass near 390 grams per mole. Because the chain is short and carries no modifications, it is assembled readily by solid-phase synthesis and is distributed mainly as a freeze-dried solid for laboratory work. Catalogue listings use the spellings epitalon, epithalone, and simply AEDG, and the three refer to the same sequence.
The compound is generally presented as a synthetic fragment of epithalamin, a pineal gland extract investigated in the former Soviet Union from the 1970s onward. Vladimir Khavinson and colleagues in Saint Petersburg developed short peptides modelled on such extracts, and epitalon became the most widely cited of those sequences. Most primary reports appeared in Russian-language journals or in proceedings with limited international circulation. Independent replication in laboratories outside that network remains sparse, and much repeated secondary material traces back to a small number of originating groups.
Laboratory work has examined effects on telomerase activity in cultured cells, on melatonin rhythms in animals, and on markers of oxidative stress. Some experiments report measurable changes while others show none, and the reported findings rest largely on small studies. The absence of large independent trials means the generality of these results is unresolved rather than settled. Review articles occasionally apply the label geroprotector, a term that reflects a research hypothesis about ageing rather than an established clinical finding.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Derived from the four-residue sequence |
| Molar mass | About 390.35 g/mol | Free peptide, counter-ion not included |
| Appearance | White to off-white powder | Lyophilised solid from aqueous solution |
| Water solubility | Freely soluble | Short, polar peptide chain |
| Common synonyms | AEDG; epithalone | Catalogues use the names interchangeably |
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.
The compound is generally described as a synthetic analogue of a fragment isolated from a pineal gland extract. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology introduced it during the 1980s and 1990s while studying short peptides from animal tissue. The original extract, called epithalamin, is a heterogeneous mixture, whereas epitalon is a single defined sequence. That distinction matters because findings reported for the extract are not automatically findings about the pure tetrapeptide, and claims about broader biological effects remain a separate question from the chemical identity described here.
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.
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.
== Literatur == Isabelle Flury: Glycosylphosphatidylinositol Membrane Anchors in Saccharomyces cerevisiae: Characterization of Proteins Involved in Side Chain Modifications. (PDF; 5,9 MB), Dissertation. Universität Freiburg in der Schweiz, 2001.
Granula sind unter dem Mikroskop deutlich sichtbare, körnchenförmige Einlagerungen in biologischen Zellen, die meist Speicher- oder Sekretstoffe enthalten (z. B. Glykogen-, Lipid-, Protein-, Ferritin- oder Pigment-Granula). Umgeben sind sie von einer Nicht-Einheitsmembran, die den Granulainhalt vom Cytoplasma ausgrenzt. Sie lassen sich anhand ihrer Anfärbbarkeit unterscheiden in: azidophil, azurophil, basophil, chromaffin, eosinophil, metachromatisch und neutrophil. Die Freisetzung von Granula aus den Zellen nennt man Degranulation. Ansammlungen von beispielsweise fehlerhaft gefalteten Proteinen nennt man dagegen Einschlusskörperchen.
Das große T-Antigen (LTag oder LT, von engl. large ‚groß‘ und Tumor-Antigen) ist ein onkogenes und DNA-bindendes Protein des Simian-Virus 40 (SV40). Es wird in der Biochemie und Zellbiologie zur Immortalisierung von Säugetier-Zellen verwendet. Homologe kommen in anderen Polyomaviren vor, mit Längen zwischen 600 und 800 Aminosäuren.
Sources: de.wikipedia.org
== Eigenschaften == Das große T-Antigen dient dem SV 40 zur Regulierung der viralen Replikation. Weiterhin transformiert es die Wirtszelle. Es wird als replikationsrelevantes Protein zu Beginn des viralen Replikationszyklus gebildet (im Gegensatz zu den Kapsidproteinen) und ist essentiell für die virale Replikation. Neben der Immortalisierung und der Transformation führt das große T-Antigen zu einer gestörten Differenzierung, zum Verlust der DNA-Reparatur und zu einer Instabilität des Karyotyps. Das große T-Antigen bringt ruhende Zellen zur Zellteilung durch Überwindung der Checkpoints der Zelle. Dabei bindet es an pRB (synonym RB1) und p53 und bewirkt die Dissoziation des Elongationsfaktors E2F1 von pRB, wodurch die Genexpression von E2F1-regulierten Genen der S-Phase eingeleitet wird. Die Bindung an pRB und p53 erzeugt die transformierende Wirkung. Daneben hemmt das große T-Antigen die Bindung von p53 an DNA, wodurch p53 an der Aktivierung der Genexpression gehemmt wird. Bei der Erforschung des großen T-Antigens wurde p53 im Jahr 1979 entdeckt. Das große T-Antigen wirkt in der Einleitung der Transkription analog zu TAF (TFIID-assoziierter Faktor) für alle drei zellulären RNA-Polymerasen durch Stabilisierung des TBP-TFIIA-Proteinkomplexes an Promotoren. Weiterhin hemmt es die HDAC1-vermittelte Deacetylierung von Histonen, wodurch die Transkription aktiviert wird. Zudem fördert es die Aktivierung des Promotors von Cyclin A über seine J-Proteindomäne. Vermutlich hemmt es die wachstumshemmende Wirkung der E3-Ubiquitinligase Cul7.
Sources: de.wikipedia.org
It is a synthetic tetrapeptide built from alanine, glutamate, aspartate and glycine. The four residues are joined by standard peptide bonds, giving a linear chain rather than a branched structure.
The name derives from epithalamin, a pineal gland extract studied in the former Soviet Union. Researchers proposed that short fragments of that extract carried the biological activity of interest.
No major regulatory agency has approved it as a medicine. It is handled as a research chemical, and products sold under this name are not standardised drugs with defined clinical labelling.
It is a four-amino-acid peptide with the sequence alanine-glutamate-aspartate-glycine. The chain is unmodified and contains only standard proteinogenic residues, which makes it straightforward to produce by solid-phase synthesis and to characterise by standard peptide methods.