Vilon

Vilon is a synthetic dipeptide and the shortest member of the Khavinson bioregulator series developed at the St Petersburg Institute of Bioregulation and Gerontology. PubChem indexes it as CID 7010502, L-lysyl-L-glutamic acid, with the molecular formula C11H21N3O5, a molecular weight of 275.30 g/mol and CAS number 45234-02-4. Research-grade material is supplied as a lyophilized (freeze-dried) solid. Two residues is the practical floor for anything described as a peptide, and that length shapes every part of the analytical work, from how the compound retains on a column to how it is detected.

The sequence is not in dispute, which sets Vilon apart from several compounds in this series, but the literature search is. Lys-Glu is an ordinary dipeptide that appears throughout nutrition and food chemistry under names such as lysylglutamic acid, and a search on the chemical name returns a great deal that has nothing to do with the bioregulator programme. The trade name Vilon and the shorthand KE are the reliable search handles. The same dipeptide is reported as a component of the Thymalin preparation (PubMed 37686182), linking the extract generation to the synthetic one.

The programme began in the 1970s with polypeptide complexes prepared from animal organs, thymus among them, later reduced to minimal synthetic fragments. Vilon is the dipeptide from that effort, and its earliest PubMed-indexed appearance is a 2000 report on tumour incidence and lifespan in mice (PubMed 10944717).

A microarray study examined gene expression in mouse heart after exposure to Vilon and Epitalon (PubMed 12360356), a Tbilisi group reported chromatin decondensation in lymphocytes from older donors (PubMed 15105581), and a 2022 Italian collaboration tested Vilon with four other Khavinson peptides in a human monocyte line (PubMed 35408963).

The record is thin and largely closed. PubMed returns roughly 74 items for Vilon as a peptide, nearly all from the St Petersburg programme or its collaborators, most of them English translations of Russian originals in one journal. The Tbilisi and Italian reports are the nearest thing to outside work, and there is no published human trial, pharmacokinetic data or toxicology package.

The mechanism proposed for this class is transcriptional: very short peptides are said to enter cells and nuclei, associate with regulatory regions of DNA, and shift gene expression. For Vilon the supporting observations are a microarray survey of mouse heart transcripts (PubMed 12360356) and chromatin decondensation in lymphocytes from older donors (PubMed 15105581). Neither establishes a binding site, and the proposal remains an argument, not settled biochemistry.

A distinction worth holding is Vilon against Thymogen. Both are dipeptides from this programme and both are reported among the components of Thymalin, but Vilon is Lys-Glu and Thymogen is Glu-Trp: different masses, different charge, and only one aromatic residue between them. Nor should Vilon be equated with Thymalin, an undefined extract rather than a single molecule.

The methodology caveat is size. A dipeptide is close to the products of ordinary protein digestion, so separating an administered compound from background peptide is difficult, and no published work establishes its stability in a living animal. The rodent lifespan studies used small groups and were not independently replicated.

Sealed lyophilized Vilon is held frozen at -20°C, shielded from light, in its original container. Lyophilized peptides are hygroscopic, so a container is allowed to reach ambient temperature before opening.

Repeated freeze-thaw cycles are avoided. Stability for a lot is documented on its Certificate of Analysis.

Reconstitution means returning a lyophilized compound to solution. No preparation procedure appears here: solvent and concentration belong to a study protocol. Vilon carries a free carboxyl side chain and a free amino side chain, an amphoteric and highly polar molecule handled as aqueous-soluble material.

Neither lysine nor glutamic acid is aromatic, so Vilon has no chromophore near 280nm. Solubility and water-content figures for a lot appear on its Certificate of Analysis.

Identity and purity of research-grade Vilon are established by reverse-phase HPLC and mass spectrometry. Verified purity is documented per lot on the Certificate of Analysis, and with no aromatic residue, identity rests on low-wavelength detection and mass confirmation.

Very short, highly polar peptides retain poorly on standard reverse-phase columns, so method matters. Counter-ion content, acetate or trifluoroacetate, also shifts measured mass.

Vilon is the shortest member of a bioregulator group from one programme.

• Thymalin.
  The thymus polypeptide preparation reported to contain this dipeptide.
• Pinealon.
  The tripeptide Glu-Asp-Arg, one residue longer with a basic arginine.
• Cartalax.
  Indexed as the tripeptide Ala-Glu-Asp, acidic rather than amphoteric.
• Epitalon.
  The tetrapeptide Ala-Glu-Asp-Gly, the most published member of the series.

Khavinson VKh, Anisimov VN (2000). A synthetic dipeptide vilon (L-Lys-L-Glu) inhibits growth of spontaneous tumors and increases life span of mice. Dokl Biol Sci.
PubMed 10944717

Anisimov SV, Boheler KR, et al. (2002). Studies of the effects of Vilon and Epithalon on gene expression in mouse heart using DNA-microarray technology. Bull Exp Biol Med.
PubMed 12360356

Lezhava T, Khavinson V, et al. (2004). Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people. Biogerontology.
PubMed 15105581

Avolio F, Martinotti S, et al. (2022). Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line. Int J Mol Sci.
PubMed 35408963

Linkova N, Khavinson V, Diatlova A, et al. (2023). The Influence of KE and EW Dipeptides in the Composition of the Thymalin Drug on Gene Expression and Protein Synthesis Involved in the Pathogenesis of COVID-19. Int J Mol Sci.
PubMed 37686182

Vilon is stocked in one format from one supplier brand: a single sealed lyophilized vial listing at a 20mg fill. Vials are the only listed format for this compound, and per-vial strengths are product specifications only. Each lot is batch tested with a published Certificate of Analysis documenting verified purity and identity for that lot.

• Browse all Vilon research products
• Verified Peptides Vilon, 20mg lyophilized vial

These products are sold for Research Use Only and are not intended for human consumption.