Ovagen Peptide Description
This research-grade Ovagen lyophilized peptide complex provides laboratories with high-purity bioregulator material for liver and gastrointestinal tract investigations. The Khavinson developed tripeptide demonstrates specific affinity for hepatic tissue research applications.
Each peptide vial delivers consistent results through rigorous quality control and independent testing protocols. Manufactured in USA facilities using the highest standards, this peptide bioregulator supports liver function studies and cellular research.
Third-party verified purity ensures reliable experimental outcomes for qualified research institutions. Strictly for in vitro research applications only.
Peptide Information
| Property |
Value |
| Peptide Sequence |
H-Glu-Asp-Leu-OH |
| Molecular Formula |
Cโโ
Hโโ
NโOโ |
| Molecular Weight |
375.37 g/mol |
| PubChem CID |
444128 |
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 ฮผM. 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 ฮผM[1].
References
- J. M. Louis, F. Dyda, N. T. Nashed, A. R. Kimmel, and D. R. Davies, โHydrophilic Peptides Derived from the Transframe Region of Gag-Pol Inhibit the HIV-1 Protease,โ American Chemical Society (ACS), Feb. 1998. doi: 10.1021/bi972059x. https://doi.org/10.1021/bi972059x
