What Vesugen Is
Vesugen is a synthetic tripeptide, Lys-Glu-Asp (KED), C15H26N4O8, 390.39 g/mol. Within the peptide bioregulator family it is classified as vascular-associated.
KED is the structural hub of this family. Three other catalog compounds are the same tripeptide with one residue added: Prostamax is KED + proline, Livagen is KED + alanine, and Pancragen is KED + tryptophan. That makes Vesugen the natural reference point for any question about how a single added residue changes behaviour.
Research use only. Supplied for laboratory research. Not for human or veterinary use. No marketing authorisation exists and no therapeutic claim is made.
What the Published Literature Contains
No PubMed-indexed study names Vesugen in its title. There is no compound-specific work establishing a biological effect, a mechanism tied to this sequence, a safety profile, or an amount for any species.
The class-level literature describes short peptides generally: the systematic review of peptide regulation of gene expression (Khavinson et al., Molecules 2021, PMID 34834147), and work on a vascular peptide preparation and microvascular density in aged rat brain cortex (Sokolova et al., Bull Exp Biol Med 2016, PMID 27383168).
That second paper is the one most often cited as if it were a Vesugen study. It is not: it concerns a vascular peptide preparation within the same programme, not KED under this name. The distinction matters when the vascular association is being used as a premise.
The Contrast Worth Designing Around
Pancragen — KED plus a single tryptophan — has six papers naming it, including primate work. Vesugen has none. One residue separates the best-documented compound in this family from one with no compound-specific literature at all.
If the research question is whether the family's tissue assignments track sequence or are conventional labels, that pair is the cleanest available comparison.
Structure and Handling
- Sequence. Lys-Glu-Asp (KED), tripeptide.
- Formula. C15H26N4O8, 390.39 g/mol.
- Form. Lyophilised powder, ≥98% purity, third-party certificate of analysis per batch.
- Storage. Sealed vial at −20 °C, protected from light; reconstituted solution at 2–8 °C.
- Reconstitution. Bacteriostatic water down the vial wall, never onto the powder cake. Do not shake. See the reconstitution calculator.
Related Compounds
Do not confuse Vesugen with Vesilut: they are different molecules — Vesilut is the dipeptide Glu-Asp. For compounds with substantive published work see Vilon, Pancragen and Epithalon. Full family on the bioregulator overview.
KED-Family Evidence Map: Comparative Documentation Across Four Compounds
Because Vesugen (KED) is the structural core of four catalog compounds, the most informative framing is not a Vesugen-specific literature review — none exists — but a systematic comparison of documentation depth across the family. The table below maps each compound against its PubMed-indexed evidence base as of mid-2025. All four share the Lys-Glu-Asp backbone; the differentiating residue is noted.
| Compound | Sequence | Tissue Association (label) | Indexed Studies (approx.) | Best-Documented Model | Compound-Specific PMID Available? |
|---|---|---|---|---|---|
| Vesugen (KED) | Lys-Glu-Asp | Vascular | 0 (compound-specific) | None identified | No |
| Prostamax (KEDP) | Lys-Glu-Asp-Pro | Prostate | ~2–3 | Aged rat prostate tissue | Limited; class-level attribution applies |
| Livagen (KEDA) | Lys-Glu-Asp-Ala | Liver / immune | ~3–4 | Murine immunosenescence models | Yes, limited |
| Pancragen (KEDW) | Lys-Glu-Asp-Trp | Pancreas | ~6 | Primate; aged rat pancreas | Yes, most robust in family |
Two points follow directly from this map. First, the tissue assignments — vascular for KED, prostate for KEDP, pancreas for KEDW — are labels inherited from the Khavinson programme's organ-extract origins, not conclusions derived from sequence-activity studies of these synthetic tripeptides independently.[3] Whether the C-terminal residue (Pro, Ala, Trp) is the determinant of tissue tropism, or whether the assignments reflect the tissue from which the parent polypeptide extract was prepared, is an open question with no published answer. Second, the Pancragen–Vesugen pair is the cleanest within-family contrast available to a researcher: one residue of difference, six-fold difference in documentation depth. Any study designed to ask what the tryptophan residue contributes would use these two compounds as the minimal pair.
The vascular-preparation work most commonly cited in connection with Vesugen (Sokolova et al., 2016) examined microvascular density in aged rat brain cortex using a peptide preparation from vascular tissue, not synthetic KED.[4] That distinction is preserved in the table above and should be preserved in any research protocol that draws on it.
Proposed Mechanism at the Class Level — and Where It Stops
No study has characterised a receptor, binding partner, or intracellular cascade for Lys-Glu-Asp specifically. What exists is a mechanistic framework proposed for short peptide bioregulators as a class, articulated most completely in the Khavinson et al. 2021 systematic review in Molecules.[3] The proposed mechanism operates at the chromatin level: short di- and tripeptides — particularly those with basic residues capable of interacting with negatively charged DNA phosphates — are hypothesised to enter the nucleus and influence histone–DNA contacts, thereby modulating local transcription. Lys (basic, +1 charge at physiological pH) at the N-terminus of KED is structurally consistent with this model. Glu and Asp (both acidic) introduce a charge asymmetry that may affect binding geometry, though this is mechanistic inference rather than measured behaviour.
Epistemic status: proposed. The chromatin-interaction hypothesis has been tested in cell-free systems and in silico for short peptides as a class; it has not been tested for KED as an isolated compound in any published study. The 2021 review describes molecular docking analyses suggesting complementarity between short basic peptides and promoter regions of genes associated with cellular ageing, but docking studies constitute computational hypothesis generation, not demonstration of biological effect.[3] Extrapolating from class-level docking data to compound-specific mechanism requires direct experimental evidence that does not currently exist in the indexed literature for Vesugen.
One corollary worth noting for research design: the charge distribution of KED (net charge approximately −1 at pH 7.4, given two acidic and one basic residue) differs from the net-positive short peptides most discussed in the chromatin-interaction literature. If the mechanism depends on electrostatic complementarity with DNA, KED's net charge may predict weaker or geometrically distinct interaction relative to peptides such as Lys-Glu (net neutral) or purely basic sequences. This is a testable prediction that the literature has not yet engaged. Any in vitro programme examining KED's transcriptional effects would be generating primary data rather than confirming established findings.
Inference from Structural Analogs: What the KED-Extended Compounds Contribute — and What They Cannot
Because no PubMed-indexed study names Vesugen (KED) as its primary compound, any mechanistic inference must travel from the analog literature. That transfer carries a specific evidentiary cost that should be stated explicitly rather than absorbed into prose.
The closest documented analog is Pancragen (KED-Trp), which has been examined in pancreatic and retinal models in rodents and, in at least one report, in primates. Livagen (KED-Ala) has been examined in the context of chromatin decompaction in lymphocyte preparations. Prostamax (KED-Pro) has associated literature in prostate epithelial cell contexts. In each case the published biological activity is attributed to the tetrapeptide — not to the shared KED core — and no study in this group includes a KED-alone arm or a KED-deletion control that would allow the contribution of the tripeptide core to be isolated from the contribution of the fourth residue.
The systematic review by Khavinson et al. (Molecules, 2021) [5] surveyed short-peptide regulation of gene expression across the bioregulator programme and described a general model in which di- and tripeptides interact with gene promoter regions, particularly GC-rich domains, through intercalation or groove-binding interactions modeled computationally. That review covers the class mechanism; it does not report a Vesugen-specific binding event or a KED-specific gene target. Citing it as evidence for a Vesugen effect requires an assumption — that the tripeptide core of each analog is the pharmacophore — that has not been tested with a controlled experiment in any published work indexed in PubMed.
The in silico modeling work within the Khavinson programme, summarized in part by Ryzhak et al. and related authors across multiple publications in the Bulletin of Experimental Biology and Medicine, proposes docking of short peptides to DNA promoter sequences as a class mechanism. [6] These models are computationally derived; no published study has reported direct binding measurements for KED specifically using techniques such as surface plasmon resonance, isothermal titration calorimetry, or fluorescence anisotropy. The proposed mechanism is therefore correctly classified as proposed — mechanistic reasoning without direct experimental confirmation for this compound — and should not be described in the same register as a measured outcome.
For a research program attempting to use Vesugen as a reference point for the KED family, the most defensible experimental design would include both KED and at least one KED-extended analog as parallel conditions, rather than inferring KED behavior retrospectively from analog results.
Regulatory Status, Research Classification, and Documentation Gaps
Vesugen carries no marketing authorization in any jurisdiction. No IND (Investigational New Drug) application, IMPD (Investigational Medicinal Product Dossier), or equivalent regulatory submission for KED as an isolated compound is reported in public regulatory databases as of the date of this article. It therefore has no approved indication, no established human dose, no validated safety profile, and no regulatory-grade pharmacokinetic dataset.
Within research classification frameworks, KED is a synthetic peptide of defined sequence and known molecular formula (C₁₅H₂₆N₄O₈, MW 390.39 g/mol). Its CAS registry status should be confirmed against ChEBI or PubChem at the point of procurement, as short peptides with overlapping trivial names occasionally carry conflicting registry entries across databases — a discrepancy class documented elsewhere in this catalog. Researchers sourcing the compound should verify sequence, purity method (HPLC), and counterion specification in the certificate of analysis before use.
The absence of clinical-phase regulatory documentation means that any extrapolation from the class-level or analog literature to human pharmacology lacks the bridging data — species-to-human PK/PD scaling, safety margins, receptor occupancy at achievable concentrations — that regulatory review would normally require. This is not a criticism of the compound; it is the accurate description of where the documentation stops.
For comparative context: the broader peptide bioregulator programme has produced one compound, Epithalamin/Epitalon (Ala-Glu-Asp-Gly), with a more substantial clinical-era publication record, including reports in Russian-language journals indexed in PubMed, though that compound's evidence base has also been critically assessed as methodologically heterogeneous. [7] The vascular-tissue association assigned to Vesugen appears to derive from the original Khavinson tissue-specificity framework rather than from independent experimental validation of that assignment for the KED sequence specifically. [5]
Institutions considering KED in a research context should treat it as a novel chemical entity with class-level mechanistic hypotheses and no compound-specific human or regulatory data. Ethics review bodies and institutional biosafety committees are likely to apply a novel-compound framework rather than a precedented-class framework, because the analog data is insufficient to establish a read-across that a regulatory agency would accept without additional bridging studies.
