The short version of AEDG tetrapeptide fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2026-04-11 and is reviewed periodically as new material appears.
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.
The proposed relationship between epitalon and pineal function is a central part of its background. Khavinson's group reported that short peptides corresponding to regions of larger pineal proteins could influence gene expression in cells. Epitalon was framed as a synthetic analogue of an active fragment rather than a direct isolation product. Whether the tetrapeptide reproduces the effects of the parent extract is an open question, because comparative studies are limited and the parent extract itself is not a single defined substance.
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.
| Property | Value | Notes |
|---|---|---|
| Amino acid sequence | Ala-Glu-Asp-Gly | Tetrapeptide, often abbreviated AEDG |
| Molecular formula | C14H22N4O9 | Free peptide, unmodified termini |
| Molecular weight | ~390.35 Da | Calculated for the free acid form |
| Appearance | White to off-white powder | Typical lyophilized product form |
| Solubility class | Freely soluble in water | Two acidic residues dominate ionic character |
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.
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Sources: en.wikipedia.org
Inborn errors of metabolism form a large class of genetic diseases involving congenital disorders of enzyme activities. The majority are due to defects of single genes that code for enzymes that facilitate conversion of various substances (substrates) into others (products). In most of the disorders, problems arise due to accumulation of substances which are toxic or interfere with normal function, or due to the effects of reduced ability to synthesize essential compounds. Inborn errors of metabolism are often referred to as congenital metabolic diseases or inherited metabolic disorders. Another term used to describe these disorders is "enzymopathies". This term was created following the study of biodynamic enzymology, a science based on the study of the enzymes and their products. Finally, inborn errors of metabolism were studied for the first time by British physician Archibald Garrod (1857–1936), in 1908. He is known for work that prefigured the "one gene–one enzyme" hypothesis, based on his studies on the nature and inheritance of alkaptonuria. His seminal text, Inborn Errors of Metabolism, was published in 1923.
==== Neurotransmission and neuromodulation ==== Extensive production of TRH throughout the CNS various non-endocrine (neurotransmissive and neuromodulatory) functions. Indeed, artificial administration into the CNS exhibits autonomic (hyperthermic, hypertensive, positive chronotropic, and gastrokinetic effects, and promotion of insulin and gastric acid release), antiepileptic, anxiolytic, and pro-locomotive effect.
Citing the Shafer report, a lobbying campaign from 1973 to 1978, spearheaded by the National Organization for the Reform of Marijuana Laws (NORML), convinced 11 states to decriminalize cannabis for personal use. In 1973, Nixon created the Drug Enforcement Administration (DEA) by an executive order accepted by Congress, to "establish a single unified command to combat an all-out global war on the drug menace." The agency was charged with enforcing US controlled substances laws and regulations nationally and internationally, coordinating with federal, state and local agencies and foreign governments, and overseeing legally produced controlled substances. The DEA absorbed the Bureau of Narcotics and Dangerous Drugs, ODALE, and other drug-related federal agencies or personnel from them.
Sources: en.wikipedia.org
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.
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.
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.
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.