N-Acetyl Epithalon

Product Details: N-Acetyl Epithalon Peptide

N-Acetyl Epithalon is a synthetic tetrapeptide composed of aspartic acid, glutamic acid, aspartic acid, and alanine (Asp-Glu-Asp-Ala), modified with an N-terminal acetyl group. This modification is commonly used in peptide chemistry to improve stability by reducing susceptibility to enzymatic degradation in in vitro systems. [1]

It is typically supplied as a lyophilized powder, allowing accurate reconstitution and consistent handling in laboratory environments. The acetylated structure supports controlled experimental conditions where peptide stability and reproducibility are required. [1]

While the parent peptide Epithalon has been investigated in experimental models, direct studies on the N-acetylated variant remain limited. As such, this compound is primarily used in research settings to evaluate how structural modifications influence peptide behavior and biochemical interactions. [2]

Mechanism of Action

N-Acetyl Epithalon is a modified analog of Epithalon, and its mechanism is inferred based on studies of the parent peptide. Experimental research on Epithalon suggests its involvement in telomerase-related pathways, including modulation of telomerase activity and chromatin-associated processes in cell-based models. [2][3]

However, direct mechanistic studies on the N-acetylated form are currently limited. The addition of the acetyl group is primarily associated with enhanced peptide stability and resistance to proteolytic cleavage, rather than altering the core biological targets of the peptide. [1]

Due to this modification, N-Acetyl Epithalon is investigated in laboratory settings for its potential to maintain consistent molecular interactions over extended experimental conditions.

Properties of N-Acetyl Epithalon Peptide: 

• Molecular Formula: C16H24N4O10
• Molecular Weight: 432.38 g/mol
• CAS Number: Not available
• PubChem CID: 171390141
• Synonyms: N-Acetyl Epitalon, UXR7AF6R4F, RefChem:1091504

Research Applications/Benefits of N-Acetyl Epithalon Peptide

• Telomerase-Related Research Models: Studies on the parent peptide Epithalon indicate its involvement in telomerase-associated pathways and chromatin regulation in experimental systems. The N-acetylated variant is used in research to explore whether structural modification influences these mechanisms under controlled conditions. [2][3]
• Peptide Stability and Proteolytic Resistance Studies: N-terminal acetylation is widely investigated for its ability to enhance peptide stability and reduce enzymatic degradation, supporting reproducibility in biochemical and cell-based assays. [1]
• Epigenetic and Chromatin Interaction Studies: Epithalon-derived peptides are explored in experimental models for their association with chromatin structure and gene regulation. The acetylated form may be used to assess how peptide modifications affect these interactions. [2]

References: 

1. Li, D., Yang, Y., Li, R., Huang, L., Wang, Z., Deng, Q., & Dong, S. (2021). N-terminal acetylation of antimicrobial peptide L163 improves its stability against protease degradation. Journal of Peptide Science, 27(9), e3337.
2. Khavinson, V. K., & Malinin, V. V. (2005). Peptides and aging. Neuroendocrinology Letters, 26(2), 139–144.
3. Khavinson, V. K., Linkova, N. S., Dyatlova, A. S., et al. (2017). Epigenetic regulation of gene expression and telomere length by short peptides. Advances in Gerontology, 7(3), 201–208

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