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Free U.S. shipping on orders over $150Vilon is a short synthetic dipeptide composed of lysine bound to glutamic acid (Lys-Glu).
Vilon is considered a thymic peptide analogue, meaning it mimics biological activity associated with peptides produced by the thymus gland, an organ essential to immune system development.
Like other bioregulatory peptides, Vilon has been studied for its ability to regulate protein synthesis and normalize cellular homeostasis, particularly in tissues affected by stress, aging, or immune dysfunction.
While Vilon is not approved for medical use outside research settings, its small molecular structure enables high bioavailability and cell membrane permeability, characteristics that have made it an important subject in peptide-based therapy research.
Vilon shows immunomodulatory properties, particularly its effects on thymus-dependent immune pathways.
In an in vitro study using human monocytic THP-1 cells, Vilon treatment resulted in [1]:
In Type 1 diabetes patients, administering Vilon resulted in [2]:
Vilon has been investigated within the field of bioregulatory peptide research for its potential role in cellular repair, longevity regulation, and tissue regeneration.
A case series examined 250 adults aged 65–87 with chronic periodontitis along with type II diabetes, atherosclerosis, and other cardiovascular diseases. Subjects received 10–20 µg daily submucosally for 5–10 days. The treatment significantly improved immune, oxidative stress, and coagulation parameters. Vilon treatment also reduced periodontal pocket depths by 1.2 Ramfjord index points and papillary marginal alveolar index by 10 times. These benefits, however, happened to a lesser degree in younger people with chronic periodontitis [3].
Age-associated declines in phosphorylated CREB (pCREB) reduce levels of arylalkylamine N-acetyltransferase (AANAT), contributing to age-related declines in melatonin, circadian rhythm, and sleep disruption.
Rat pinealocytes were treated with either control (no treatment), norepinephrine (NE) 1 µg/ml (positive control), or peptide-treated cultures (epithalone or Vilon) at 100 ng/ml. Subsequently, cultures were incubated for up to 3 hours at 36.7°C in 5% CO2 [4].
Results showed that Vilon:
Vilon peptide transiently enhances early transcriptional activation (pCREB) and enzyme induction (AANAT) in pinealocytes, suggesting it plays a regulatory role in stimulating melatonin synthesis at the initial phase of the signaling cascade.
Aging is often associated with increased chromatin condensation (heterochromatinization), which suppresses gene expression.
Another cell study investigated the effects of Vilon on chromatin organization in cultured lymphocytes obtained from elderly individuals [5]. The results demonstrated that Vilon loosened chromatin both globally and in the nucleolus, restoring access to genes silenced during aging.
Vilon plays an apoptoregulatory role, helping to protect somewhat damaged healthy cells. However, in cancer cells, Vilon seems to increase apoptotic cell death, which can help prevent further cancer progression.
In a cell study, administration of Vilon administered to rat spleen lymphocytes post-radiation induced significantly less apoptosis [6]. To date, the exact mechanisms by which apoptosis is inhibited has not been elucidated.
In rats transplanted with carcinoma, Vilon stimulated apoptosis in both young and old rats, suggesting that instead of protecting damaged cells, Vilon plays a more apoptoregulatory role [7].
Because dysregulated apoptosis is a hallmark feature of carcinogenesis, some studies have explored Vilon’s effects in oncological research settings.
Early experimental reports from Russian investigators suggest that Vilon could serve as an adjuvant to cancer therapy, resulting in [8]:
However, such studies remain experimental, and no clinical evidence currently supports Vilon for use in oncology.
Vilon’s role in apoptoregulation continues to be a subject of research in the broader field of cellular homeostasis and peptide-based cytoprotection.
Research Use Only. All findings described above are derived from preclinical studies (animal models and in vitro experiments). Vilon is not approved by the FDA for any diagnostic or therapeutic use in humans. Genesis Peptides makes no claims regarding human clinical efficacy. This product is sold exclusively for laboratory research.
Every lot undergoes six independent assays before release. Results are published in the lot-specific Certificate of Analysis.
Vilon, also called Lys-Glu, is a dipeptide and one of the Khavinson peptides. The Khavinson peptides, including Vilon, were initially isolated from animal tissues and found to be organ specific. In a study on human embryo bone marrow mesenchymal stem cells grown in culture, the Lys-Glu (KE) dipeptide was one of the short peptides examined for effects on the expression of several genes. In an in vitro study on human THP-1 monocytic cells, Vilon was one of five Khavinson peptides tested as regulators of inflammatory and proliferative processes. The available studies are therefore laboratory cell studies, and they do not cover all research on Vilon.
A review lists Vilon among the natural and synthetic peptide thymomimetics (thymalin, thymogen, vilon, epithalamin, cortexin) discussed for their immunopharmacological effect and clinical use. The same review describes Vilon as a peptide thymomimetic, a peptide bioregulator that mimics thymus hormone activity, and notes its use in the complex treatment of dental diseases in the elderly.
In an in vitro study using terminally differentiated THP-1 cells, Vilon inhibited the expression of TNF and IL-6 stimulated by LPS. The authors concluded that the Khavinson peptides, including Vilon, act as anti-inflammatory molecules on macrophages, based on these cell-culture results.
In a human observational study, Vilon (Lys-Glu) was one of four differentially expressed metabolites in seminal samples that showed exceptional diagnostic potential for primary idiopathic male infertility. In the same study of men with primary idiopathic infertility and fertile controls, Lys-Glu showed a negative correlation with sperm motility.
In a human observational study of semen samples, Vilon (Lys-Glu) was detected by untargeted liquid chromatography-mass spectrometry (LC-MS) metabolomics profiling. In those seminal samples, Lys-Glu was one of four differentially expressed metabolites that showed exceptional diagnostic potential, with an AUC above 0.97, for primary idiopathic male infertility.
Sirtuin-6 expression in 'young' and 'old' skin fibroblast cultures was studied using immunofluorescence confocal microscopy. In these in vitro cultures, Vilon increased the sirtuin-6 expression area by 1,6 and 2,6 times in young and old skin fibroblasts, respectively.
In grass carp, the group fed a 0.5% KE diet showed significant differences in muscle fiber diameter and density compared with the control group, where KE is the Lys-Glu dipeptide that Vilon contains. In these fish, muscle fiber diameter and density were also negatively correlated with each other. Compared with the control diet, the Lys-Glu dipeptide (KE) of Vilon inhibited the expression of the protein metabolism genes AKT, S6K1 and FoxO1a in grass carp, but promoted PCNA expression.
In laying hens, hens fed 45 mg Fe/kg as Fe-Lys-Glu had higher yolk iron content than hens given the same dose of FeSO4. In laying hens, Fe-Lys-Glu supplementation at 30 to 75 mg Fe/kg increased red blood cell count and hemoglobin content compared with the control group.
FOR RESEARCH USE ONLY — Products are sold exclusively for in vitro and preclinical laboratory research. Not for human consumption or administration. Not intended for diagnostic or therapeutic use. These statements have not been evaluated by the FDA.