Vilon

Vilon (Lys-Glu, also written KE or lysylglutamic acid) is a synthetic dipeptide developed by Prof. Vladimir Khavinson and colleagues at the St. Petersburg Institute of Bioregulation and Gerontology. At Verified Peptides, we place Vilon in Khavinson's "cytogen" product line — single, defined-sequence synthetic peptides engineered to reproduce what the institute's researchers identified as the active fragment of a corresponding natural tissue extract — distinguishing it from "cytomax" natural multi-peptide complexes such as Glandokort, also built on this site. Vilon's sequence was identified through amino acid analysis of Thymalin, an earlier natural thymus-gland extract already used in Soviet-era clinical settings for immune modulation; Khavinson's team isolated Lys-Glu as one of the components proposed to be responsible for Thymalin's immune-cell effects.

Chemically, Vilon is a straightforward two-residue peptide: molecular formula C11H21N3O5, molecular weight approximately 275.3 g/mol, CAS number 45234-02-4, PubChem CID 7010502. Its small size is a defining feature of this entire peptide-bioregulator research program — proponents describe it as small enough to cross cell membranes and enter the nucleus without depending on classical receptor-mediated signaling, allowing direct interaction with chromatin and DNA.

Vilon is one of the more extensively published members of Khavinson's peptide-bioregulator catalog, with research spanning immune-cell culture studies, rodent tumor and lifespan studies, and — more recently — an international, peer-reviewed collaborative study. We think this makes it a genuinely more evidenced compound than some other names in this same research family, though, as detailed below, the great majority of that evidence still originates from or includes the peptide's own developing institute.

At Verified Peptides, we think Vilon's evidence base, while still originating overwhelmingly from one research lineage, is more substantial than some other Khavinson-associated compounds in this catalog, and we want to walk through it directly. The earliest indexed research we located is Khavinson and Anisimov's 2000 paper in Doklady Biological Sciences (PMID 10944717), which reported that subcutaneous Vilon administration to female CBA mice beginning at six months of age increased physical activity, modestly prolonged lifespan, and reduced spontaneous tumor incidence compared to untreated controls. These are real, indexed, published findings — but they come from a single rodent strain, a single research lineage, and describe modest effect sizes rather than dramatic ones.

A more recent cell-culture study, "Immunomodulating effects of Vilon and its analogue in the culture of human and animal thymus cells" (Sevostianova et al., Bulletin of Experimental Biology and Medicine, 2013, PMID 23486604), examined Vilon's effects on cultured thymus cells directly, again conducted at the St. Petersburg Institute of Bioregulation and Gerontology. This and the 2000 paper share the same institutional origin as Vilon's own development, which is an important limitation: research demonstrating a compound's effects conducted by the same group that developed and commercially promotes it carries an inherent conflict-of-interest consideration that independent replication would resolve, but has not yet, to our knowledge, been resolved for Vilon specifically.

The most methodologically reassuring citation we located is a 2022 study in the International Journal of Molecular Sciences (Avolio et al., PMID 35408963), examining Vilon and four other Khavinson peptides in the human THP-1 monocyte/macrophage cell line. This study's primary institutional affiliation is the University "G. d'Annunzio" in Chieti-Pescara, Italy — a genuinely independent academic institution — though Khavinson and colleagues from his own institute are listed as co-authors, meaning this is best described as an international collaborative study rather than a fully independent third-party replication. It nonetheless represents Vilon's clearest published presence in a Western, broadly indexed, peer-reviewed international journal, distinguishing it from compounds in this catalog whose only evidence sits entirely within Russian-language or institute-internal sources.

We are not aware of any registered or published human clinical trial for Vilon, and no FDA, EMA, or other Western regulatory body has evaluated or approved it for any indication. At Verified Peptides, we sell research-grade Vilon exclusively for laboratory research, and we encourage researchers to weigh its rodent and cell-culture evidence, and the institutional relationships behind that evidence, carefully rather than assuming the peptide-bioregulator framework's broader claims apply uniformly to every compound in the catalog.

Vilon's discovery lineage illustrates how several of Khavinson's "cytogen" peptides came to exist: rather than being newly discovered peptides, they were identified through amino acid analysis of earlier natural tissue extracts already used clinically in Soviet medicine, such as Thymalin (a thymus extract) in Vilon's case. Khavinson's group proposed that Lys-Glu was the specific fragment of Thymalin responsible for at least some of its immune-modulating clinical effects, then developed it as a standalone synthetic dipeptide, following the same general "cytomax-to-cytogen" pattern used across the institute's broader bioregulator research program.

Vilon is one of only two amino acids joined by a single peptide bond, making it among the structurally simplest compounds in this entire catalog. This simplicity is central to the mechanistic claims made about it — proponents argue that its small size allows it to bypass classical receptor-based signaling and enter the nucleus directly, a claim that, if broadly true across such a minimal structure, would represent an unusual mode of peptide action compared to most receptor-mediated peptide hormones and growth factors described elsewhere in this catalog.

The 2022 International Journal of Molecular Sciences study examining Vilon in THP-1 cells tested it alongside four other Khavinson peptides in the same cell-culture system, allowing for at least some internal, side-by-side comparison of these compounds' effects under identical experimental conditions — a methodological improvement over evaluating each peptide only in isolation across different studies and labs, though the comparison remains confined to this one paper and one cell line.

Vilon is sold commercially as a research compound in both lyophilized injectable-format vials and, in some markets, informally associated with broader "Vilon" branded supplement or capsule products; researchers should confirm exactly which formulation and grade they are receiving, since commercial branding in this space is not always precise about distinguishing research-grade synthetic peptide from other preparations.

Vilon is frequently confused with, or discussed alongside, Thymogen (Glu-Trp), a separate Khavinson thymic dipeptide with a different two-amino-acid sequence and its own distinct research history. Both are described as thymus-derived immunomodulatory dipeptides and both emerged from the same broader Soviet-era thymic-extract research program, but researchers should treat them as two structurally and mechanistically distinct compounds rather than interchangeable names for the same peptide, since their published effects and specific research literatures are not identical.

The original natural extract Thymalin, from which Vilon's sequence was derived, has itself been used in Soviet and Russian clinical contexts for immune correction in settings such as post-surgical recovery, burn injury, and radiation exposure — a considerably broader historical clinical use case than Vilon, the isolated dipeptide, has itself accumulated independent evidence for. This distinction between Thymalin's older, broader clinical use history and Vilon's narrower, more recent, single-fragment research profile is worth keeping separate when evaluating claims about either compound.

At Verified Peptides, we require independent third-party HPLC purity testing and mass spectrometry identity confirmation for every batch of research-grade Vilon we offer, with a Certificate of Analysis (COA) available for each lot. As a simple two-residue dipeptide, Vilon is straightforward to synthesize to high purity via standard peptide-synthesis methods, but batch verification remains important for any research relying on consistent, reproducible results.

We source exclusively from manufacturers operating under Good Manufacturing Practice (GMP)-aligned quality systems, and every lot is independently verified rather than accepted solely on a supplier's internal documentation. Researchers should always request and review the specific COA for the lot they receive, confirming purity percentage and molecular identity before use in any experimental protocol.

Lyophilized Vilon is stable when stored at -20°C, protected from light and moisture, and researchers can generally expect the unreconstituted peptide to maintain integrity over an extended period under these conditions. At Verified Peptides, we ship lyophilized peptide with appropriate cold-chain packaging to preserve stability in transit.

Once reconstituted with bacteriostatic water or another appropriate sterile diluent, Vilon solution should be stored refrigerated at 2–8°C and used within the timeframe indicated on the product's documentation. As a very small dipeptide, Vilon is generally considered chemically stable relative to larger, more structurally complex peptides, but reconstituted solutions remain more susceptible to degradation and microbial contamination than the lyophilized form, particularly with repeated freeze-thaw cycling.

Researchers should avoid repeated freeze-thaw cycles of reconstituted material and should follow the specific storage guidance provided with each lot's documentation to preserve sample validity for research use.