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Epitalon Peptide Background And Structure — Field Notes

By Editorial Desk · published 2026-04-24 · last reviewed 2026-06-01 · Faq

Everything below concerns bioregulator. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.

Updated 2026-06-01. Numbers and descriptions here follow the published literature rather than marketing material.

Epitalon Peptide Background and Structure

Epitalon is a synthetic tetrapeptide with the amino acid sequence alanine-glutamate-aspartate-glycine, abbreviated Ala-Glu-Asp-Gly or AEDG. It was developed by the Russian researcher Vladimir Khavinson and colleagues during work on peptide bioregulators derived from the pineal gland. The compound is short enough to be produced by standard solid-phase peptide synthesis and is typically handled as a lyophilized white powder. Its small size distinguishes it from larger pineal peptides such as epithalamin, a complex extract from which the tetrapeptide was conceptually derived.

The four residues give epitalon a molecular formula of C14H22N4O9 and a molecular weight near 390.35 daltons. The presence of two acidic residues, glutamate and aspartate, makes the free peptide strongly acidic, while the alanine and glycine ends provide neutral, nonpolar character. This combination produces a molecule with substantial water solubility. Because there are no cysteine, methionine, or tryptophan residues, the peptide lacks the most common oxidation-sensitive side chains, which simplifies handling compared with many longer peptides.

Identity and Research Background

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.

Epitalon at a glance

PropertyValueNotes
Amino acid sequenceAla-Glu-Asp-GlyTetrapeptide, often abbreviated AEDG
Molecular formulaC14H22N4O9Free peptide, unmodified termini
Molecular weight~390.35 DaCalculated for the free acid form
AppearanceWhite to off-white powderTypical lyophilized product form
Solubility classFreely soluble in waterTwo acidic residues dominate ionic character

Epitalon Background and Nomenclature

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.

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Background from the literature

== Siehe auch == Hepatologie Leberpunktion LiMAx-Test Calot-Dreieck Campolon Kratzauskultation Leberhautzeichen, Leberfleck (Hautveränderungen) Leberparenchym Gallenfarbstoffe Gallenstein Leberbalsam, Leberblümchen, Lebermoos (Pflanzen) Leberbrand (Viehkrankheit) Leberschau (Hepatoskopie) „Säuferleber“ bei einer Alkoholkrankheit

== Literatur == Wolfgang F. Caspary u. a. (Hrsg.): Therapie von Leber- und Gallekrankheiten. Springer-Verlag, Berlin 2000, ISBN 3-540-67390-3. Helmut Denk u. a.: Pathologie der Leber und Gallenwege. (= Spezielle pathologische Anatomie. Band 10). Springer-Verlag, Berlin 2000, ISBN 3-540-65511-5. Hansludwig Hagen: Die physiologische und psychologische Bedeutung der Leber in der Antike, Rheinische Friedrich-Wilhelms-Universität Bonn, 1961. Erwin Kuntz, Hans-Dieter Kuntz: Praktische Hepatologie. Historie, Morphologie, Biochemie, Diagnostik, Klinik, Therapie. Barth, Heidelberg 1998, ISBN 3-335-00568-6. Ellen Schmidt u. a. (Hrsg.): Lebererkrankungen. Pathophysiologie, Diagnostik, Therapie. Wissenschaftliche Verlagsgesellschaft, Stuttgart 2000, ISBN 3-8047-1640-7. Hans Adolf Kühn: Krankheiten der Leber. In: Ludwig Heilmeyer (Hrsg.): Lehrbuch der Inneren Medizin. Springer-Verlag, Berlin/Göttingen/Heidelberg 1955; 2. Auflage ebenda 1961, S. 847–875. Renate Lüllmann-Rauch: Taschenlehrbuch Histologie. Georg Thieme Verlag, Stuttgart 2006. Nikolaus Mani: Die historischen Grundlagen der Leberforschung; I: Die Vorstellungen über Anatomie, Physiologie und Pathologie der Leber in der Antike; II: Die Geschichte der Leberforschung von Galen bis Claude Bernard. Basel und Stuttgart 1959 und 1967 (= Basler Veröffentlichungen zur Geschichte der Medizin und der Biologie, 9 und 21). Heiner Wedemeyer: Das Leber-Buch. Wie halte ich meine Leber gesund? Neue Therapien und Stand der Forschung.

Grundlagen der Leberfunktion leberinfo.de elektronenmikroskopische Abbildungen der Leber - EM Atlas im Internet Diseases of the Liver (engl.) Sonographiebilder Ultraschall-Atlas der Leber SonoAtlas Ein Ultraschallatlas der Leber

Sources: de.wikipedia.org

Reference notes

Somatostatin ist ein Peptidhormon in Wirbeltieren, das u. a. von der Bauchspeicheldrüse (Pankreas) während der Verdauung ausgeschüttet wird und als Inhibiting-Hormon des Hypothalamus die Bildung des Wachstumshormons Somatropin in der Hypophyse hemmt. Daher kommt auch das Synonym somatotropin (release)-inhibiting hormone (SIH bzw. SRIH) oder auch growth hormone (release)-inhibiting hormone (GHIH bzw. GHRIH). Außerdem nimmt es an der Signaltransduktion bei der Einleitung der Apoptose teil. Synthetische Analoga des Somatostatins sind Lanreotid, Pasireotid und Octreotid, welche als Arzneistoffe zugelassen sind. Ein früher als Bulbogastron bezeichnetes Peptid ist wahrscheinlich identisch mit Somatostatin. Somatostatin wird nicht nur von den δ-Zellen der Bauchspeicheldrüse gebildet, sondern auch von einzelnen Zellen des Hypothalamus und des Gastrointestinaltrakts. Es ist ein wichtiger Regulator des Hormon- und Nervensystems und wirkt durch Bindung an G-Protein-gekoppelte Rezeptoren (GPCRs) auf der Oberfläche verschiedener Zelltypen. Erstmals isoliert wurde Somatostatin 1972 von Roger Guillemin aus dem Hypothalamus von 490.000 Schafen. Somatostatin hemmt die Sekretion von Pankreasenzymen, Gastrin und Pepsin und senkt die Durchblutung im Splanchnikusgebiet (Versorgungsgebiet der Eingeweidenerven Nervus splanchnicus major und Nervus splanchnicus minor).

Sources: de.wikipedia.org

Frequently asked questions

What is epitalon made of?

Epitalon is a synthetic tetrapeptide composed of four amino acids: alanine, glutamate, aspartate, and glycine. It is written as Ala-Glu-Asp-Gly. The free peptide has a molecular weight of about 390 daltons and is normally supplied as a lyophilized powder.

Is epitalon extracted from the pineal gland?

No. Epitalon is chemically synthesized, not extracted. It was designed as a short synthetic fragment conceptually related to larger pineal peptides studied in the same research tradition, particularly the extract known as epithalamin. The two are distinct materials with different compositions.

Why is epitalon described as a bioregulator?

The term bioregulator is used in this research tradition for short peptides proposed to influence gene expression or cell function. Epitalon is grouped with other synthetic short peptides under this label. The term reflects a proposed mechanism rather than an established drug classification.

What is epitalon?

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.

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