tetrapeptide 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.
Last reviewed on 2026-08-01. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
Verification of research-grade material involves comparing a supplier chromatogram against an in-house reference, checking the observed mass against the calculated value, and where possible confirming residue order by tandem mass spectrometry or enzymatic peptide mapping. Purity claims should be read alongside the method used to obtain them, because detection wavelength and integration settings alter the result. Batch-specific data, rather than a generic grade statement, is the informative part of a certificate.
Identity and purity of epitalon samples are normally established by reversed-phase high-performance liquid chromatography with ultraviolet detection near 214 nanometres, combined with mass spectrometry. The mass spectrum confirms the expected molecular ion and can reveal truncated or oxidised by-products. Amino acid analysis after acid hydrolysis verifies that the four residues are present in the expected ratio. Certificates typically report a purity figure taken from chromatographic peak area, expressed as a percentage of total integrated signal.
Lyophilised epitalon is generally held at minus twenty degrees Celsius in a sealed container kept dry and dark. Cooler conditions are sometimes recommended for long-term archives. The solid takes up moisture readily enough that repeated opening of a vial introduces water, so dividing a batch into smaller portions before storage lowers degradation risk. Aqueous solutions are less durable than the dry powder and are usually prepared shortly before use, then kept cold and shielded from light to slow hydrolysis and oxidation.
| Property | Value | Notes |
|---|---|---|
| Peptide sequence | Ala-Glu-Asp-Gly | Often abbreviated AEDG in research literature |
| Common synonyms | Epithalon, epitalon, AEDG | Spelling variants refer to the same tetrapeptide |
| Molecular formula | C14H22N4O9 | Theoretical monoisotopic mass near 390.35 Da |
| Appearance | White to off-white powder | Typically supplied as a lyophilised solid |
| Solubility class | Freely soluble in water | Hydrophilic peptide; dissolves in aqueous buffer |
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.
Identity is normally established by reversed-phase high-performance liquid chromatography combined with mass spectrometry, a pairing that separates components and confirms molecular mass at once. Purity is quoted as a percentage from the chromatogram, and figures above ninety-five percent are a frequent commercial specification. Amino acid analysis or sequencing supplies further confirmation when required. Because many short peptides behave similarly under chromatography, retention time alone does not establish sequence; the mass measurement is what separates one tetrapeptide from another, and certificates should report both.
Short peptides such as AEDG are normally supplied as a freeze-dried solid and are kept dry, cold, and shielded from light. Holding at minus twenty degrees Celsius is common for the long term, while a refrigerator suffices for brief periods before use. The material takes up moisture to some degree, so containers should stay sealed and be allowed to reach room temperature before opening, which limits condensation on the contents. Repeated warming and cooling of a single container is discouraged because it admits water and can lower the amount of intact peptide.
== Nomenclature == The first member of this gene family was called p10, in reference to the size and molecular weight (in kDa) of a protein from insect regenerating legs. The same protein (called Pam) was found in the adult antennae and legs from the two sexes of the American cockroach P. americana [2, 35]. Similar clones identified in Drosophila and Locusta in a search for olfactory genes referred to Olfactory-Sensory type D protein (OS-D or Pheromone Binding Protein A10) [20, 46-47]. Related clones identified in the antennae of the sphingid Manduca sexta were named sensory appendage proteins (SAPs) to distinguish them from a family of longer six-cysteine soluble proteins, i.e. odorant-binding proteins or OBPs [48]. Individual SAPs/CSPs have been designated in various ways: p10/Periplaneta americana (Nomura et al., 1992) [35], A10/Drosophila melanogaster (Pikielny et al., 1994) [46], OS-D/D. melanogaster (McKenna et al., 1994) [47], Pam/P. americana (Picimbon & Leal, 1999) [2], CSP/Schistocerca gregaria (Angeli et al., 1999) [3], SAP/Manduca sexta (Robertson et al., 1999) [48], Pherokine/D. melanogaster (Sabatier et al., 2003) [33], B-CSP/Acinetobacter baumannii, Macrococcus caseolyticus, Kitasatospora griseola, Escherichia coli (Liu et al., 2019) [24]. The protein family was renamed to chemosensory protein (CSP) by Angeli et al. after one (polyclonal) antibody against p10 labeled some sensory structures in the adult antennae of the desert locust Schistocerca gregaria [3]. The term “B-CSP” was used to refer to similar clones from bacterial (B) species [24].
radiochemistry The branch of chemistry involving the study of radioactive substances and radioactivity, including the use of radioactive isotopes to study non-radioactive isotopes and ordinary chemical reactions.
Although the following examples illustrate the diversity of point-mutation–mediated disorders, there are over 300,000 such mutations recorded in HGMD and over 1,000,000 variants in ClinVar, reflecting the vast spectrum of human point mutations.
=== EC 2.7.9: Phosphotransferases with paired acceptors (dikinases) === EC 2.7.9.1: pyruvate, phosphate dikinase EC 2.7.9.2: pyruvate, water dikinase EC 2.7.9.3: selenide, water dikinase EC 2.7.9.4: α-glucan, water dikinase EC 2.7.9.5: phosphoglucan, water dikinase EC 2.7.9.6: rifampicin phosphotransferase
The relatively quick heteronuclear single quantum correlation experiment helps determine the feasibility of doing subsequent longer, more expensive, and more elaborate experiments. It is not possible to assign peaks to specific atoms from the heteronuclear single quantum correlation alone.
Sources: en.wikipedia.org
=== AC-driven === LEDs developed by Seoul Semiconductor can operate on AC power without a DC converter. For each half-cycle, part of the LED emits light and part is dark, and this is reversed during the next half-cycle. The efficiency of this type of HP-LED is typically 40 lm/W. A large number of LED elements in series may be able to operate directly from line voltage. In 2009, Seoul Semiconductor released a high DC voltage LED, named 'Acrich MJT', capable of being driven from AC power with a simple controlling circuit. The low-power dissipation of these LEDs affords them more flexibility than the original AC LED design.
DNA usually occurs as linear chromosomes in eukaryotes, and circular chromosomes in prokaryotes. The set of chromosomes in a cell makes up its genome; the human genome has approximately 3 billion base pairs of DNA arranged into 46 chromosomes. The information carried by DNA is held in the sequence of pieces of DNA called genes. Transmission of genetic information in genes is achieved via complementary base pairing. For example, in transcription, when a cell uses the information in a gene, the DNA sequence is copied into a complementary RNA sequence through the attraction between the DNA and the correct RNA nucleotides. Usually, this RNA copy is then used to make a matching protein sequence in a process called translation, which depends on the same interaction between RNA nucleotides. In an alternative fashion, a cell may copy its genetic information in a process called DNA replication. The details of these functions are covered in other articles; here the focus is on the interactions between DNA and other molecules that mediate the function of the genome.
== Enzyme activity == In many of the species containing lactate racemase, the physiological role of the enzyme is to convert substrate D-lactate into L-lactate. In other species, such as L. plantarum, the cellular role is to transform L-lactate into D-lactate for incorporation into the cell wall. The in vitro reaction catalyzed by the enzyme reaches equilibrium at the point where approximately equimolar concentrations of the D- and L-isomers exist. L. plantarum initially produces L-lactate, which induces the activity of lactate racemase. By contrast, D-lactate represses lactate racemase activity in this species. Therefore, Lar activity appears to be regulated by the ratio of L-lactate/D-lactate. L. plantarum LarA represents a new type of nickel-dependent enzyme, due to its novel nickel-pincer ligand ligand cofactor.
==== Deficit in consolidation of memory traces ==== α-CaMKII heterozygous mice express half the normal protein level as the wild-type level. These mice showed normal memory storage in the hippocampus, but deficits in consolidation of memory in the cortex.
Sources: en.wikipedia.org
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.
No. Epithalamin is a peptide-rich extract prepared from bovine pineal glands, while epitalon is a short synthetic peptide designed as a defined analogue of it. The synthetic version was intended to provide a reproducible molecule with some of the same proposed biological activity.
Telomere elongation and telomerase activation have been reported in cultured human somatic cells, but evidence from living human subjects is limited and has not been independently confirmed at scale. Reported findings come largely from small studies with differing designs, so the question remains open rather than settled.
The usual approach is reversed-phase HPLC with ultraviolet detection, reported as a percentage of total peak area. Mass spectrometry is used alongside chromatography to confirm identity rather than purity alone.