Everything below concerns Epitalon. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Updated 2026-06-23. Numbers and descriptions here follow the published literature rather than marketing material.
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.
Epitalon is a synthetic tetrapeptide whose sequence is alanine-glutamate-aspartate-glycine, written in single-letter code as AEDG. The four residues are joined by three peptide bonds, giving a linear backbone with no branching and no disulfide bridges. Its calculated molecular mass for the free form is approximately 390.3 daltons, a figure that rises when the compound is supplied as an acetate or trifluoroacetate salt. Because the chain is short, the molecule is defined entirely by its residue order rather than by any folded three-dimensional structure.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Free acid form of the tetrapeptide |
| Molecular mass | About 390.35 Da | Calculated monoisotopic value |
| Appearance | White to off-white powder | Typical lyophilized presentation |
| Solubility | Soluble in water | Also dissolves in buffered saline |
| Storage temperature | Minus 20 degrees Celsius | Dry, dark conditions; avoid repeated thawing |
Literature searches for this compound must account for several spelling variants. Indexing databases contain epitalon, epithalon, epithalone, and AEDG, and relevant records are scattered across Russian-language and English-language journals that do not consistently cross-cite. Early publications describe the parent extract as a mixture of many peptides, whereas later work addresses the single synthetic tetrapeptide. That shift in nomenclature complicates comparison between studies, because extract data and tetrapeptide data are sometimes cited interchangeably. A search strategy omitting the alternate spellings will return an incomplete set of references.
Reported biological findings come mainly from cell culture and rodent experiments. Those studies describe changes in telomerase catalytic subunit expression, melatonin rhythm amplitude, and antioxidant enzyme activity after peptide exposure. Human data are sparse and consist of small trials with limited blinding and inconsistent endpoints. The proposed mechanisms remain hypotheses rather than established facts, and there is no consensus on whether effects observed in animals carry over to people. Independent replication outside the original research groups is limited, which is a recognised gap in the published literature.
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.
Hydrophobic membranes are often polydimethylsiloxane based where the actual separation mechanism is based on the solution-diffusion model described above. Hydrophilic membranes are more widely available. The commercially most successful pervaporation membrane system to date is based on polyvinyl alcohol. More recently also membranes based on polyimide have become available. To overcome the intrinsic disadvantages of polymeric membrane systems ceramic membranes have been developed over the last decade. These ceramic membranes consist of nanoporous layers on top of a macroporous support. The pores must be large enough to let water molecules pass through and retain any other solvents that have a larger molecular size such as ethanol. As a result, a molecular sieve with a pore size of about 4 Å is obtained. The most widely available member of this class of membranes is that based on zeolite A. Alternatively to these crystalline materials, the porous structure of amorphous silica layers can be tailored towards molecular selectivity. These membranes are fabricated by sol-gel chemical processes. Research into novel hydrophilic ceramic membranes has been focused on titania or zirconia. Very recently a break-through in hydrothermal stability has been achieved through the development of an organic-inorganic hybrid material.
12(S)-HpETE and 12(S)-HETE induce itching responses when injected into the skin of mice; this has led to the suggestion that these metabolites contribute to the itching (i.e. clinical pruritus) which accompanies such conditions as atopic dermatitis, contact dermatitis, urticaria, chronic renal failure, and cholestasis. Since it mediates 12(S)-HETE-induced itching in the mouse model, BLT2 rather than GPR31 may mediate human itch in these reactions.
== Spectrum of bacterial susceptibility and resistance == Cefpodoxime has been used to treat gonorrhoea, tonsillitis, pneumonia, and bronchitis. The following minimum inhibitory concentrations have been reported:
Sources: en.wikipedia.org
their intensive labouring demands and time consumption their confinements by the definition of the term defined by different standards. To solve this kind of difficulty, some regulatory bodies or methods provide advice on when performing of a specified system suitability test should be applied and compulsory.
Dipeptides are white solids. Many are far more water-soluble than the parent amino acids. For example, the dipeptide Ala-Gln has the solubility of 586 g/L more than 10x the solubility of Gln (35 g/L). Dipeptides also can exhibit different stabilities, e.g. with respect to hydrolysis. Gln does not withstand sterilization procedures, whereas this dipeptide does. Because dipeptides are prone to hydrolysis, the high solubility is exploited in infusions, i.e. to provide nutrition.
Hand therapy is often recommended. Approximately six weeks after surgery the patient is able completely to use the hand. The average recurrence rate is 39% after a fasciectomy after a median interval of about four years.
Sources: en.wikipedia.org
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.
No naturally occurring free form of the peptide has been described. The four-amino-acid sequence can appear as a fragment within larger proteins, but that is not the same as the intact compound being present as a circulating molecule. Materials used in research are synthetic.
Purity is usually checked by reverse-phase high-performance liquid chromatography, which separates the target peptide from related impurities. Mass spectrometry is commonly used alongside it to confirm molecular mass. Some suppliers also provide amino acid analysis for additional sequence confirmation.
The peptide contains four residues in the order alanine, glutamate, aspartate and glycine, abbreviated AEDG. The chain is linear and held together by three peptide bonds. Its calculated mass for the uncharged free form is about 390.3 daltons.