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 2025-12-01 and is reviewed periodically as new material appears.
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.
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 a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and its calculated monoisotopic mass is approximately 390.35 daltons. The compound does not occur naturally as a free peptide; it is produced by solid-phase peptide synthesis. Because it contains two acidic residues and no basic residues, the neutral form carries a net negative charge at physiological pH. This charge profile influences how the peptide behaves in solution and during chromatographic analysis.
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.
| 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 |
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.
Discussions in the literature often conflate three distinct entities: the pineal extract epithalamin, the isolated tetrapeptide AEDG, and commercial preparations sold under similar names. Reviews citing older Russian-language studies sometimes omit detail on purity, route of administration and control groups, which makes cross-study comparison difficult. Researchers working with the compound generally note the need for independent replication, standardized enzyme assays, and clearer reporting of peptide identity. These caveats are relevant when weighing claims that appear in secondary sources rather than in primary reports.
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9, and its calculated molar mass is approximately 390.35 grams per mole. The compound is a short fragment related to a peptide fraction isolated from bovine pineal gland extracts, and it is normally supplied as a lyophilised powder intended for laboratory research. It is not a registered pharmaceutical product in most countries.
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.
=== Dry co-micronization === Dry co-micronization is a nanomilling approach in which the drug substance is milled in a dry state together with GRAS excipients in a single unit operation. The excipients form a protective dispersion matrix around the sub-micron drug particles, preventing the surface-energy-driven reaggregation that otherwise dominates dry submicron powders, and yielding a free-flowing powder that can be tableted or encapsulated without further drying or downstream processing. The most widely commercialized dry co-micronization platform is SoluMatrix Fine Particle Technology, developed by iCeutica and acquired in 2011 by Iroko Pharmaceuticals. The platform has been used to formulate three U.S. Food and Drug Administration–approved low-dose non-steroidal anti-inflammatory drugs: Zorvolex (diclofenac, approved October 2013), Tivorbex (indomethacin, approved February 2014), and Vivlodex (meloxicam, approved October 2015). Each product was approved at a total daily dose 20–35% below the equivalent conventionally-formulated NSAID, on the basis that the increased dissolution rate of sub-micron particles permits comparable analgesic efficacy at lower systemic exposure. Unlike wet media milling, dry co-micronization requires no aqueous suspension or downstream drying step, shortening the unit-operation chain at the cost of constraining the formulation to excipients compatible with high-energy dry impact.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Half-Life: Opposing Force is an expansion pack for the first-person shooter game Half-Life (1998). It was developed by Gearbox Software and published by Sierra On-Line for Windows on November 19, 1999. Opposing Force was the first expansion for Half-Life and was announced in April 1999. Lead designer Randy Pitchford believed Gearbox was selected to develop Opposing Force because Valve, the creators of Half-Life, wanted to concentrate on their future projects. Over the course of development, Gearbox brought in a variety of talent from other areas of the video games industry to help bolster various aspects of design. Opposing Force portrays the events of Half-Life from the perspective of a U.S. Marine, one of the enemy characters in the original, assigned to the Hazardous Environment Combat Unit (HECU). The player character, Adrian Shephard, is sent in to neutralize the Black Mesa Research Facility when a scientific mishap causes it to be invaded by aliens, but quickly finds that the Marines are outnumbered and slowly being beaten back by a second alien race and black operations units. Opposing Force was received well by critics, with many describing it as the new benchmark title for expansion packs, in a similar fashion to how Half-Life revolutionized the first-person shooter genre. Other reviewers, however, thought that, despite its accomplishments, it still suffered from the negative aspects of other expansion packs.
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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.
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.