What is Vesugen?
Vesugen has the molecular formula C16H28N4O9 and a molecular weight of 420.42, with three residues. No CAS registry number is assigned in our molecular dataset, so none is quoted. The sequence combines a basic lysine with glutamate and aspartate, producing a small zwitterionic molecule with essentially no hydrophobic surface, which makes it very water soluble and difficult to retain on a reverse-phase column without an ion-pairing agent.
The bioregulator family comes from Vladimir Khavinson and colleagues at the St Petersburg Institute of Bioregulation and Gerontology, who reduced organ-derived peptide fractions to the shortest synthetic sequences that remained active in their assays. The proposed mechanism for these cytogens is that a two to four residue peptide penetrates the nucleus and binds promoter-region DNA or histone proteins, changing transcription of genes linked to the source tissue.
This remains a hypothesis. The molecular support consists mainly of docking simulations and spectroscopic binding measurements from the originating laboratories, no crystal structure of a short peptide bound to a specific promoter has been published, and independent replication of the transcriptional claims is sparse. What is established is the chemistry, the stability of the dried solid, and that Vesugen is the tripeptide core of the related tetrapeptide Testagen.
Reconstitution & handling
The powder dissolves almost immediately in bacteriostatic or sterile water added slowly down the vial wall, since a 420 dalton tripeptide with three ionizable side chains is among the most soluble materials here. Concentration is the labeled milligram content divided by the diluent volume. Gentle swirling is enough, as a three-residue peptide has no folded structure to disturb.
Storage & stability
Sealed vials are stored at -20 degrees Celsius, protected from light and from atmospheric moisture, since the cake is hygroscopic and a softened cake indicates seal failure. Reconstituted material is held at 2 to 8 degrees Celsius, split into single-use aliquots, and kept out of repeated freeze-thaw cycles. The sequence contains no cysteine, methionine or tryptophan, so oxidation is not a meaningful liability, and slow backbone hydrolysis sets the practical limit on solution shelf life.
How it's tested
Purity is measured by reverse-phase HPLC at 214 and 220 nanometres, typically with an ion-pairing agent, because a highly polar tripeptide with no aromatic residue elutes near the void volume on an unmodified C18 gradient. Identity is confirmed by mass spectrometry against the theoretical average mass of 420.42. Net peptide content is determined so the labeled figure reflects peptide rather than counter-ion and residual water.