Livagen Peptide 20mg

Livagen is the synthetic tetrapeptide Lys-Glu-Asp-Ala (KEDA), one of the short peptides from Vladimir Khavinson’s bioregulator programme in St Petersburg and usually sold in the West as a liver peptide. This listing is a 20 mg vial of freeze-dried Livagen, formula C18H31N5O9. Most of what has been published on it concerns chromatin: how it changed the packing of chromosomes in lymphocytes cultured from elderly donors, in work by Khavinson’s institute and a collaborating cytogenetics group in Tbilisi.

Specifications

Livagen's place in the series

Livagen is a straight chain of four residues with free ends: lysine, glutamic acid, aspartic acid and alanine. The safety data sheet gives the formula as C18H31N5O9, and the Livagen guide puts the mass at about 461.5 g/mol. It has one basic side chain, two acidic ones and no aromatic ring. Three of its residues are shared with testagen, which is Lys-Glu-Asp-Gly¹, so the two peptides differ only at the C-terminus, alanine against glycine. Livagen is often confused with Ovagen, the tripeptide Glu-Asp-Leu, but they differ in length and composition, and the guide points out that the Khavinson organisation’s own synthetic range lists Ovagen, not Livagen, as its liver product.

Handling notes

Going by its composition, Livagen has no methionine or cysteine to oxidise, no asparagine to deamidate and no tryptophan to degrade under light, points the Livagen guide makes in its section on degradation chemistry. That does not make it indifferent to storage. Keep the sealed vial at −20 °C, the temperature the safety data sheet gives for peptides, desiccated and dark, and let it reach room temperature before opening so that moisture does not condense on the powder. The sheet puts reconstituted solutions at 2 to 8 °C, protected from light, for a period your laboratory has established.

What the research covers

Where Livagen comes from

Livagen belongs to the synthetic short peptides of Khavinson’s programme. Anisimov and Khavinson’s 2010 review describes the approach: small peptides were isolated from different organs and tissues, and di-, tri- and tetrapeptide analogues were then synthesised from amino acids². The group’s account of how such peptides act is set out in a 2021 systematic review, in which chains of two to seven residues enter nuclei and nucleoli, interact with nucleosomes, histones and DNA, and regulate gene expression and DNA methylation³. Fluorescence work by Fedoreyeva and colleagues showed labelled short peptides, testagen among them, reaching the nucleus and nucleolus of HeLa cells¹. Livagen is not named in that abstract.

Chromatin in lymphocytes from elderly donors

The measured findings for Livagen come from cytogenetics. Khavinson, Lezhava and Malinin exposed leukocytes from people aged 75 to 88 to five synthetic peptides: Vilon, Epithalon, Livagen, Prostamax and Cortagen⁴. All five activated ribosomal genes, loosened densely packed chromatin and released genes that had been silenced by age-related condensation. Livagen was one of three peptides that decondensed the pericentromeric heterochromatin of chromosome 1, and one of two, with Epithalon, that also changed chromosome 9⁴.

Lezhava and Jokhadze followed this up in cultured lymphocytes from donors aged 80 to 91, with a group aged 18 to 30 as controls⁵. They found that chromosome condensation increased with age and that Livagen reactivated condensed regions in the older donors’ cells. Cobalt chloride raised the rate of chromosomal aberrations in the old donors, and Livagen reduced the changes cobalt caused; under the combined exposure, sister chromatid exchanges were found mostly in telomeric heterochromatin⁵.

What is not established

Both chromatin studies used human cells exposed in culture, and no person received the peptide. Neither abstract measured liver cells, and none of the references on this page reports a liver outcome, an animal study or a clinical trial of Livagen. The single liver paper and the one rat study are discussed in the guide. The DNA-binding model in the 2021 review is stated for short peptides in general³ and does not show that Livagen binds a particular gene. Every Livagen study located so far shares authors with Khavinson’s institute or the Tbilisi group, and most appeared in Russian or regional journals, so the findings have not been repeated by an unconnected laboratory.

The Livagen (KEDA) guide covers the literature in more depth.

How each lot is tested

Every lot is tested in PrymaLab’s own laboratory in Ashland, Kentucky before release: RP-HPLC for purity, LC-MS for identity, Karl Fischer titration for water, LAL for endotoxin and USP <71> for sterility. Published certificates are listed on the results page and can be checked by number and key on the verify page. These are in-house results from PrymaLab Analytical, not an independent test, and the lab is not accredited to ISO 17025. The third-party testing guarantee on this page still applies: if any independent laboratory finds the wrong compound, or less than the stated purity or amount, the order is refunded and the cost of the test is reimbursed.

Frequently asked questions

References

1. Fedoreyeva LI, Kireev II, Khavinson VKh, et al. Penetration of short fluorescence-labeled peptides into the nucleus in HeLa cells and in vitro specific interaction of the peptides with deoxyribooligonucleotides and DNA. Biochemistry (Mosc). 2011;76(11):1210-9. DOI · PubMed
2. Anisimov VN, Khavinson VKh. Peptide bioregulation of aging: results and prospects. Biogerontology. 2010;11(2):139-49. DOI · PubMed
3. Khavinson VK, Popovich IG, Linkova NS, et al. Peptide Regulation of Gene Expression: A Systematic Review. Molecules. 2021;26(22). DOI · PubMed
4. Khavinson VKh, Lezhava TA, Malinin VV. Effects of short peptides on lymphocyte chromatin in senile subjects. Bull Exp Biol Med. 2004;137(1):78-81. DOI · PubMed
5. Lezhava T, Jokhadze T. Activation of pericentromeric and telomeric heterochromatin in cultured lymphocytes from old individuals. Ann N Y Acad Sci. 2007;1100:387-99. DOI · PubMed