N-Acetyl Epithalon Amidate

N-Acetyl Epithalon Amidate is a terminally modified analog of the tetrapeptide epithalon (Ala-Glu-Asp-Gly, AEDG), carrying an acetyl group on the N-terminal alanine and an amide in place of the free carboxyl group of the C-terminal glycine. The parent sequence was synthesized on the basis of the amino acid composition of epithalamin, a bovine pineal gland extract. No peer-reviewed studies indexed in PubMed were identified that examine the acetylated, amidated analog itself, so the available literature concerns the unmodified parent peptide.

N-Acetyl Epithalon Amidate in the research literature

Published work on the parent tetrapeptide has examined telomere biology in cell culture. Studies reported that unmodified AEDG induced expression of the telomerase catalytic subunit, telomerase activity and telomere elongation in telomerase-negative fetal fibroblast cultures, and a 2025 study reported hTERT mRNA upregulation and increased telomerase activity in normal epithelial and fibroblast cell lines. In rat pinealocyte culture, the parent peptide was reported to increase AANAT and pCREB synthesis. Whether terminal acetylation and amidation alter any of these activities has not been reported in the indexed literature.