Livagen peptide

Livagen peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-KEDA-OH

H-Lys-Glu-Asp-Ala-OH

4

95.27%

C₁₈H₃₁N₅O₉

461.46

Synthetic

Powder

Livagen is a tetrapeptide bioregulator with the sequence Lys-Glu-Asp-Ala. The peptide has shown high biological activity, particularly in experiments with rat liver cells. When exposed to nanomolar concentrations of Livagen, the rate of protein synthesis in hepatocyte cultures from older animals increased significantly, almost reaching the levels characteristic of young rat liver cells. Additionally, Livagen has been found to restore the intracellular circadian rhythm of biosynthesis that is often disrupted by aging.
Livagen's biological activity is of interest due to its potential role in the endogenous opioid system (EOS), which is involved in various physiological functions, including pain sensitivity, emotional reactions, learning capacity, memory, hormone secretion, and the regulation of several body systems such as respiratory, cardiovascular, digestive, and immune systems, as well as thermoregulation. In extreme cases, the EOS can mediate an increase in stress tolerance, preventing the transformation of an acute stress syndrome from a stage of adaptation to a stage of pathogenesis.
The study of Livagen's effects on the EOS focused on its ability to change the activity of enkephalin-degrading enzymes in human serum and to interact with μ- and δ-opioid receptors in the membrane fraction from rat brain. The research found that Livagen inhibits enkephalin-degrading enzymes in human serum more effectively than some well-known peptidase inhibitors, with an IC50 of 20 µM. However, it did not interact with μ- and δ-opioid receptors from the rat brain. This suggests that Livagen's mechanism of action is not through direct interaction with opioid receptors but possibly through the inhibition of enzymes that degrade endogenous opioids, which could make it a promising candidate for treating stress-induced and psychosomatic disorders.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Kost NV, Sokolov OIu, Gabaeva MV, Zolotarev IuA, Malinin VV, Khavinson VKh. Vliianie novykh peptidnykh bioreguliatorov livagena i épitalona na énkefalindegradiruiushchie fermenty syvorotki krovi cheloveka [Effect of new peptide bioregulators livagen and epitalon on enkephalin-degrading enzymes in human serum]. Izv Akad Nauk Ser Biol. 2003 Jul-Aug;(4):427-9. Russian. PMID: 12942748.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.