Price Update,Linear Tetrapeptide: Contains four residues connected by three peptide bonds

The epithalon peptide structure has garnered significant attention in scientific research, particularly within the realms of anti-aging and longevity. This fascinating molecule, also known by variations such as Epitalon, Epithalone, and Epithalon peptide, is recognized for its role as a synthetic tetrapeptide. Understanding its precise structure is crucial to appreciating its purported biological activities and potential applications.

At its core, the epithalon peptide structure is a chain composed of four specific amino acids. These amino acids are alanine, glutamic acid, aspartic acid, and glycine. This sequence is often represented as Ala-Glu-Asp-Gly (AEDG). The IUPAC name for this structure is (4S)-4-[[(2S)-2-aminopropanoyl]amino]-5-[[(2S)-3-carboxy-1-(carboxymethylamino)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid. This detailed nomenclature highlights the stereochemistry and specific linkages between the amino acid residues, forming a linear tetrapeptide. The connection between these amino acids occurs through peptide bonds, with a linear tetrapeptide containing four residues connected by three peptide bonds.

The molecular formula for epithalon is C14H22N4O9, and its molecular weight is approximately 390.35 Daltons. It is important to note that Epithalon is a synthetic peptide that was developed based on the amino acid composition of naturally occurring compounds. Specifically, it is considered a synthetic peptide derived from Epithalamin, a crude polypeptide extract of bovine pineal glands. While Epithalamin is a natural extract, Epithalon is a synthesized version designed to mimic its beneficial properties. This distinction is important when discussing its origins and applications.

The epithalon peptide structure is not just a simple arrangement of amino acids; its specific configuration is believed to be key to its interactions within biological systems. Some sources describe it as a highly bioactive pineal tetrapeptide, suggesting its origin and potent effects. The epithalon peptide structure has been linked to the concept of telomere protection. While the exact mechanism is complex, it is theorized to interact with telomerase, an enzyme that plays a role in cell division and aging. Some research suggests that telomerase contains an RNA component which supplies the telomere template for elongation, and the structure of epithalon is thought to influence this process.

The scientific community often refers to Epithalon and Epithalon interchangeably, and both terms point to this specific synthetic tetrapeptide. The research surrounding this molecule explores its potential for various benefits, including its role as a peptide for brain health and longevity. While the scientific literature is still evolving, the fundamental understanding of the epithalon peptide structure as a four-amino-acid bioregulator peptide composed of l-alanyl-l-.alpha.-glutamyl-l-.alpha.-aspartyl-glycine provides a solid foundation for further investigation into its therapeutic potential. The polarity distribution within the molecule, encompassing both polar and non-polar regions, likely contributes to its solubility and interactions with cellular components. The sequence H-Ala-Glu-Asp-Gly-O represents the N-terminus to C-terminus sequence of the peptide.

In summary, the epithalon peptide structure is a well-defined synthetic tetrapeptide with the sequence Ala-Glu-Asp-Gly. Its molecular characteristics and its origin as a synthetic analog of a naturally occurring pineal peptide underscore its significance in ongoing research into aging, cellular health, and potential therapeutic interventions.