Epitalon - Frequently Asked Questions

Epitalon is a synthetic linear tetrapeptide, classed as a Khavinson pineal bioregulator or short biologically active peptide. It is modeled on the amino-acid composition of the pineal extract epithalamin and was developed by the V.Kh. Khavinson group at the St. Petersburg Institute of Bioregulation and Gerontology.

The sequence is Ala-Glu-Asp-Gly, abbreviated AEDG, or A-E-D-G in one-letter code. It is a four-residue linear peptide with two acidic residues (glutamate and aspartate) flanked by alanine at the N-terminus and glycine at the C-terminus.

The molecular formula is C14H22N4O9 and the average molecular weight is 390.35 g/mol. These constants come from the PubChem record (CID 219042) and are what laboratory concentration and reconstitution calculations are based on.

The CAS Registry Number is 307297-39-8 and the PubChem CID is 219042. The CAS number uniquely identifies the substance across chemical databases such as ChemicalBook and BOC Sciences, and the CID links to the structural record including the canonical SMILES.

The cited models propose a direct, chromatin-level epigenetic mechanism rather than a classical receptor pathway. Fluorescently labeled AEDG penetrates the nucleus of cultured HeLa cells and binds DNA and deoxyribooligonucleotides sequence-specifically, and this is associated with modulation of gene expression, including induction of the telomerase catalytic subunit hTERT. Defined membrane-receptor and second-messenger pathways remain incompletely characterized.

Khavinson et al. (2003, PMID 12937682) reported that in telomerase-negative human fetal fibroblast cultures the peptide induces hTERT expression, increases telomerase activity by TRAP assay, and extends telomere length. A 2025 Biogerontology study (PMID 40908429) reported that telomere lengthening occurs through telomerase upregulation or, in some cancer cell lines, through alternative lengthening of telomeres (ALT).

The provided research areas are in-vitro telomerase (hTERT) regulation and telomere-length dynamics in cultured human cell lines, peptide-DNA and peptide-histone binding with proposed epigenetic gene-expression modulation, transcriptional and translational regulation of neurogenic differentiation markers in stem-cell models, antioxidant and free-radical readouts in cell and invertebrate systems, and cellular models of replicative senescence and gerontology.

Khavinson et al. (2020, Molecules, PMID 32019204) reported that AEDG increased the mRNA and protein levels of the neurogenic differentiation markers Nestin, GAP43, beta-Tubulin III, and Doublecortin in cultured human mesenchymal stem cells, which the authors framed as a possible epigenetic mechanism stimulating gene expression and protein synthesis during neurogenesis.

No half-life, clearance, or degradation kinetic value is provided in this entry, so none can be stated for Epitalon specifically. As a general peptide-class principle, a small unmodified linear tetrapeptide of 390.35 g/mol is expected to be susceptible to peptidase hydrolysis, which is one reason the cited research is conducted in controlled in-vitro systems.

For laboratory handling, the lyophilized peptide is dissolved into a defined-concentration stock, commonly using bacteriostatic water as the diluent added slowly down the vial wall with gentle swirling. Concentration is calculated from the 390.35 g/mol molecular weight; for example, 5 mg in 5 mL gives a 1 mg/mL (approximately 2.56 mM) stock. This is a research preparation workflow only, not a human dosing protocol.

All information here is strictly research-use-only and framed for in-vitro, receptor-signaling, and laboratory-research contexts. Nothing on this page constitutes a human dosing protocol, a therapeutic claim, or guidance for personal use; the reconstitution content describes laboratory preparation for in-vitro handling only.

Because the cited in-vitro work emphasizes that AEDG physically enters the nucleus and binds DNA and chromatin sequence-specifically (Fedoreyeva et al., 2011, PMID 22117547), the current models attribute its effects to direct peptide-DNA and peptide-histone interaction and downstream transcriptional modulation, rather than to a canonical surface receptor with second-messenger signaling, which remains incompletely characterized.