epitalon is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Updated 2026-01-02. Numbers and descriptions here follow the published literature rather than marketing material.
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.
The parent extract epithalamin was characterised as a low-molecular-weight fraction of pineal tissue rather than a single defined chemical entity. Researchers fractionated it and tested successive fragments for activity, a screening approach typical of peptide discovery work in that era. Epitalon emerged from that process as one of the shorter sequences of interest. Because the original extract was never fully resolved into individual components, claims about which constituent drives a given effect rest on inference. This distinction matters when reading older reports that attribute extract observations to the tetrapeptide itself.
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.
== Function == Gastric inhibitory polypeptide, also called glucose-dependent insulinotropic polypeptide, is a 42-amino acid polypeptide synthesized by K cells of the duodenum and small intestine. It was originally identified as an activity in gut extracts that inhibited gastric acid secretion and gastrin release, but subsequently was demonstrated to stimulate insulin release potently in the presence of elevated glucose. The insulinotropic effect on pancreatic islet beta-cells was then recognized to be the principal physiologic action of GIP. Together with glucagon-like peptide-1, GIP is largely responsible for the secretion of insulin after eating. It is involved in several other facets of the anabolic response.
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For many years, arsenic trioxide was administered to patients with various cancers, showing the best results in the treatment of acute promyelocytic leukemia. More than half of the patients from the first trial in Harbin survived for five years, prompting further research across other centers in China, and eventually at the Sloan-Kettering Memorial Institute in New York. The results of clinical trials were favorable enough that in 2000, the drug received FDA approval.
Sources: en.wikipedia.org
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Samples drawn from individuals with very high levels of bilirubin or lipids in their plasma (referred to as an icteric sample or a lipemic sample, respectively) may show falsely high readings for hemoglobin, because these substances change the colour and opacity of the sample, which interferes with hemoglobin measurement. This effect can be mitigated by replacing the plasma with saline. Some individuals produce an antibody that causes their platelets to form clumps when their blood is drawn into tubes containing EDTA, the anticoagulant typically used to collect CBC samples. Platelet clumps may be counted as single platelets by automated analyzers, leading to a falsely decreased platelet count. This can be avoided by using an alternative anticoagulant such as sodium citrate or heparin. Another antibody-mediated condition that can affect complete blood count results is red blood cell agglutination. This phenomenon causes red blood cells to clump together because of antibodies bound to the cell surface. Red blood cell aggregates are counted as single cells by the analyzer, leading to a markedly decreased red blood cell count and hematocrit, and markedly elevated MCV and MCHC (mean corpuscular hemoglobin concentration). Often, these antibodies are only active at room temperature (in which case they are called cold agglutinins), and the agglutination can be reversed by heating the sample to 37 °C (99 °F). Samples from people with warm autoimmune hemolytic anemia may exhibit red cell agglutination that does not resolve on warming.
==== Males ==== CPA has been found to be effective in the treatment of acne in males, with marked improvement in symptoms observed at dosages of 25, 50, and 100 mg/day in different studies. It can also halt further progression of scalp hair loss in men. Increased head hair and decreased body hair has been observed with CPA in men with scalp hair loss. However, its side effects in men, such as demasculinization, gynecomastia, sexual dysfunction, bone density loss, and reversible infertility, make the use of CPA in males impractical in most cases. In addition, lower dosages of CPA, such as 25 mg/day, have been found to be better-tolerated in men. But such doses also show lower effectiveness in the treatment of acne in men.
Sources: en.wikipedia.org
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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.