Mechanistic Claims
- Liver Function Support: Targets hepatic tissue pathways in research models.
- Immune & GI Regulation: Explored for roles in gastrointestinal tract and immune system modulation.
- Cellular Research Utility: Provides a simplified peptide model for studying bioregulatory mechanisms.
- Anti‑Aging Potential: Investigated for effects on cellular function and tissue resilience.
- Thymus & Immune Links: As part of Khavinson’s peptide library, contributes to broader immune regulation studies.
Research Applications
- Liver function and hepatocyte biology studies
- Gastrointestinal tract regulation models
- Immune system and peptide bioregulator investigations
- Cellular aging and tissue resilience research
- Exploratory anti‑aging and regenerative medicine studies
Ovagen Research Insights
- Synthetic tripeptide bioregulator with hepatic tissue affinity.
- Developed for in vitro research only; not intended for therapeutic use.
- Manufactured in USA facilities under rigorous quality control standards.
- Each batch undergoes independent third‑party purity verification for reliable outcomes.
- Supplied in lyophilized, filler‑free form to preserve integrity and extend shelf life.
Ovagen Research
HIV-1 Protease Inhibition Research
The most substantive research on the Glu-Asp-Leu tripeptide comes from HIV-1 protease inhibition studies where EDL functions as a competitive inhibitor derived from the viral transframe region (TFR). The tripeptide represents one of the smallest and most potent analogues derived from the transframe octapeptide (TFP) Phe-Leu-Arg-Glu-Asp-Leu-Ala-Phe, which naturally occurs at the N-terminus of the HIV-1 transframe region[1].
Kinetic analysis demonstrates that Glu-Asp-Leu exhibits competitive inhibition of mature HIV-1 protease with a Ki value of approximately 50 μM. This inhibitory potency is remarkable considering the tripeptide’s simple structure compared to conventional HIV protease inhibitors. The closely related tripeptide Glu-Asp-Phe shows even greater potency with a Ki value of approximately 20 μM[1].
References
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J. M. Louis, F. Dyda, N. T. Nashed, A. R. Kimmel, and D. R. Davies, “Hydrophilic Peptides Derived from the Transframe Region of Gag-Pol Inhibit the HIV-1 Protease,” American Chemical Society (ACS), Feb. 1998. doi: 10.1021/bi972059x. https://doi.org/10.1021/bi972059x
| Property | Value |
|---|---|
| Peptide Sequence | H-Glu-Asp-Leu-OH |
| Molecular Formula | C₁₅H₂₅N₃O₈ |
| Molecular Weight | 375.37 g/mol |
| PubChem CID | 444128 |