What is VILON?
Vilon is a synthetic peptide classified within the family of short "peptide bioregulators" (also referred to as Khavinson peptides), a group of low-molecular-weight oligopeptides investigated in cell-biology and molecular research. It is one of the shortest members of this class, composed of just two amino acid residues. The compound is catalogued under CAS 79443-38-8, with the molecular formula C11H21N3O6 and a molecular weight of 291.30.
Structurally, Vilon is the linear dipeptide L-lysyl-L-glutamic acid, commonly abbreviated by the single-letter amino-acid code as "KE." The molecule presents free N-terminal and C-terminal groups and comprises two residues: lysine, which contributes a basic side-chain amine, and glutamic acid, which contributes an acidic side-chain carboxyl. This combination of a cationic and an anionic residue gives the small peptide a distinctive zwitterionic, amphoteric character across physiological pH ranges. The full structure is documented on the accompanying Certificate of Analysis (COA).
As a research material, Vilon is studied in vitro as a model short-peptide bioregulator, appearing in the scientific literature on peptide-mediated gene-regulation and cellular-signaling research models. This listing describes only the physicochemical and analytical properties of the material. Vilon is offered strictly for laboratory research use only (RUO); it is not a drug, dietary supplement, cosmetic, or food, and it is not intended for human or veterinary use, diagnosis, or treatment.
Reconstitution & handling
Vilon is supplied as a lyophilized (freeze-dried) powder and is typically reconstituted in the laboratory prior to in-vitro use. As a small, highly polar dipeptide carrying both a basic lysine side chain and an acidic glutamate side chain, Vilon is readily water-soluble, and bacteriostatic or sterile water is the most common solvent for preparing an aqueous stock. The amphoteric, zwitterionic nature of the KE sequence generally supports dissolution in aqueous buffers without the need for organic co-solvents; where a specific ionic environment is required, dilute buffered systems may be used at the researcher's discretion.
To reconstitute, the solvent is directed slowly against the inner wall of the vial rather than injected directly onto the powder, and the vial is allowed to stand until the material dissolves, with gentle swirling instead of vigorous shaking to limit foaming and mechanical stress on the peptide. The resulting solution should be clear and free of visible particulates. Because small peptides are sensitive to repeated temperature cycling and microbial contamination, aqueous stocks are best prepared fresh, handled using aseptic technique, and, where appropriate, aliquoted to minimize freeze-thaw cycles.
Storage & stability
In its lyophilized form, Vilon is a stable solid best stored sealed and protected from moisture, light, and heat; short-term storage at refrigerated temperatures and long-term storage frozen (typically at or below -20 C) help preserve integrity of the freeze-dried powder. Once reconstituted, the aqueous solution is considerably less stable than the dry powder and should be kept refrigerated, protected from light, and used within a short working window. Dividing stock solutions into single-use aliquots before freezing reduces degradation associated with repeated freeze-thaw cycles. Allowing sealed vials to equilibrate toward room temperature before opening helps limit condensation on cold material.
How it's tested
The identity and purity of each Vilon lot are confirmed by analytical methods and documented on a Certificate of Analysis (COA). Reversed-phase high-performance liquid chromatography (HPLC) is used to quantify chromatographic purity, with this material specified at greater than or equal to 99%. Mass spectrometry (MS) is commonly applied to verify molecular identity by confirming the observed mass against the expected molecular weight of 291.30 for the C11H21N3O6 dipeptide, while chromatographic retention behavior supports sequence and structural confirmation. The COA consolidates these results, allowing researchers to document lot-specific identity, purity, and quality control data as part of their laboratory records.