What Vesilut Is
Vesilut — also written Vesilute, and abbreviated ED — is the dipeptide Glu-Asp, C9H14N2O7, 262.22 g/mol, catalogued as PubChem CID 99716 (L-alpha-glutamyl-L-aspartic acid).
At two residues it is among the smallest compounds in the bioregulator family, alongside Vilon (Lys-Glu) and Thymogen (Glu-Trp). It is associated with bladder tissue in the family's classification.
Research use only. Supplied for laboratory research. Not for human or veterinary use. No marketing authorisation exists and no therapeutic claim is made.
A Fragment of a Larger Sequence
The structurally interesting fact about ED is that it is contained within a longer family member: the Glu-Asp pair appears inside Prostamax (Lys-Glu-Asp-Pro), and likewise inside Vesugen (Lys-Glu-Asp), Livagen (Lys-Glu-Asp-Ala) and Pancragen (Lys-Glu-Asp-Trp).
This is worth stating carefully. Shared substructure is a reason to ask whether activity is preserved; it is not evidence that it is. A dipeptide fragment and the tetrapeptide containing it are different molecules with different size, charge distribution and conformational freedom. Any expectation that ED behaves like Prostamax is a hypothesis to test, not a finding to cite.
What the Published Literature Contains
No PubMed-indexed study names Vesilut or Vesilute in its title. No compound-specific work establishes an effect on bladder or prostate tissue, a mechanism tied to Glu-Asp, a safety profile, or an amount for any species.
The literature cited around this compound is class-level: peptide regulation of gene expression (PMID 34834147) and short peptides regulating gene expression (PMID 27909961). Neither tested ED.
What This Means for Research Design
ED is a good subject if the question is about minimal sequence length — what is the smallest fragment that retains any measurable activity within this family. It is a poor choice as a positive control or benchmark, because nothing about its own behaviour has been published.
Structure and Handling
- Sequence. Glu-Asp (ED), dipeptide.
- Formula. C9H14N2O7, 262.22 g/mol (PubChem CID 99716).
- Also known as. alpha-glutamylaspartic acid, ED, Vesilute.
- 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
Vesugen (Lys-Glu-Asp) is a different molecule and should not be confused with this one. Prostamax contains the ED pair within a longer sequence. Full family on the bioregulator overview.
Evidence Map: What Has and Has Not Been Studied in Glu-Asp Research
The table below is a structured null result. Its purpose is to prevent a common research-design error: treating the absence of a negative record as evidence of an open positive finding. For Vesilut (ED), the honest summary is that the compound has not been the named subject of any indexed pharmacological study. The entries below represent the closest published work and state precisely what each paper did and did not measure.
| Study / Year | Model | Compound Actually Tested | Outcome Measured | Key Finding | Applies to ED Directly? | Reference |
|---|---|---|---|---|---|---|
| Khavinson et al., 2016 | In vitro / cell-free transcription models; literature review | Class: short peptides (di- and tripeptides), including Lys-Glu and Glu-Trp; ED not named | Peptide–DNA binding and gene expression modulation | Short peptides proposed to interact with gene promoter regions via electrostatic complementarity; sequence-dependent specificity inferred | No. ED is not named; class-level mechanism is proposed but not measured for this compound. | [1] |
| Khavinson et al., 2021 | Literature review / bioinformatic analysis | Bioregulator peptide class broadly; individual sequences referenced vary by paper subset | Peptide regulation of gene expression in aging tissues | Short peptides associated with tissue-specific gene regulation; no bladder-specific ED data | No. Tissue association is a classification convention, not a measured outcome for ED. | [2] |
| No indexed study identified | — | Vesilut / Vesilute / Glu-Asp (ED) as named compound | Any: binding affinity, cell viability, gene expression, safety, PK | No data | Not applicable. | — |
The practical implication for researchers is direct: ED cannot currently serve as its own positive control, and no published dose, endpoint, or species model exists to anchor a study design. Any protocol must treat Glu-Asp as a novel probe with no established pharmacological baseline. The tissue classification (bladder) originates within the Khavinson bioregulator system and reflects a nomenclature convention rather than a published organ-selectivity finding.[1][2]
Dipeptide Chemistry and the Fragment Hypothesis: Structural Considerations
Vesilut is L-alpha-glutamyl-L-aspartic acid: two acidic residues joined by a peptide bond, carrying a net charge of −2 at physiological pH (pKa values of the two free carboxylates falling near 3.7 and 4.3, with the alpha-amino group near 8.0). The molecular formula C₉H₁₄N₂O₇ yields a monoisotopic mass of 262.08 Da, consistent with the PubChem record for CID 99716.[3] This charge state is significant: at pH 7.4, ED is a dianion, which has implications for membrane permeability, receptor surface complementarity, and stability in aqueous buffer.
The fragment hypothesis — the idea that a subsequence might retain some activity of the parent — is a legitimate research question in peptide biology, but it has a poor prior probability without direct measurement. The reasons are structural:
- Loss of conformational constraint. Within Vesugen (Lys-Glu-Asp) or Livagen (Lys-Glu-Asp-Ala), the Glu-Asp pair is flanked by residues that restrict its backbone dihedral angles. Isolated as a dipeptide, ED samples a broader conformational ensemble. If the parent peptide's activity depends on a specific backbone geometry, ED may not replicate it.
- Loss of the lysine residue's charge. The N-terminal Lys in Vesugen, Prostamax, and Livagen contributes a positive charge (ε-amino, pKa ~10.5) that ED lacks entirely. Electrostatic interactions proposed for peptide–DNA or peptide–receptor binding in these longer sequences cannot be assumed to survive removal of that residue.
- Different susceptibility to peptidases. Dipeptides are substrates for dipeptidyl peptidases and carboxypeptidases differently than tripeptides or tetrapeptides. Metabolic half-life in tissue homogenate is unlikely to be identical.
None of these considerations rules out activity — they rule out the assumption of activity. The fragment hypothesis is appropriately framed as: proposed, untested, with structural reasons to expect deviation from parent behavior. Researchers approaching Glu-Asp as a minimal-fragment probe should design assays against the same endpoints used for the longer family members, rather than extrapolating from parent-compound outcomes.[1]
Comparison with Neighboring Bioregulators: Identity and Evidence Tier
Vesilut belongs to a family of short bioregulator peptides developed within the same research program. The table below compares ED with its closest structural neighbors using only admissible identity facts (PubChem) and the published evidence tier documented in the primary literature. It is intended to help researchers select the appropriate compound for a given question and to make explicit where evidence exists and where it does not.
| Compound | Sequence | Formula | MW (g/mol) | Net Charge (pH 7.4) | Tissue Classification (system) | Human / Animal RCT Data? | Mechanism Proposed |
|---|---|---|---|---|---|---|---|
| Vesilut (ED) | Glu-Asp | C₉H₁₄N₂O₇ | 262.22 | −2 | Bladder (Khavinson system) | None identified | Gene expression modulation (class-level; untested for ED)[1] |
| Vilon (KE) | Lys-Glu | C₁₁H₂₁N₃O₅ | 275.30 | ~0 (zwitterionic) | Immune/thymus (Khavinson system) | Limited; mostly rodent and in vitro[1] | Immunomodulation; cytokine modulation proposed[1] |
| Thymogen (EW) | Glu-Trp | C₁₆H₁₉N₃O₅ | 337.35 | −1 | Thymus/immune (Khavinson system) | Limited human data (nasal spray formulation, immunology context)[2] | Thymopoietin-related immunomodulation proposed[2] |
| Vesugen (KED) | Lys-Glu-Asp | C₁₄H₂₄N₄O₇ | 364.36 | −1 | Vascular (Khavinson system) | None identified in indexed literature | Contains ED as C-terminal pair; longer sequence, different charge[1] |
| Prostamax (KEDP) | Lys-Glu-Asp-Pro | C₁₉H₃₁N₅O₈ | 473.48 | −1 | Prostate (Khavinson system) | Limited; Russian-language clinical reports, limited indexing[1] | Contains ED internally; Pro introduces conformational rigidity[1] |
Two patterns are visible in this comparison. First, the evidence base across the entire family is thin by the standards of Part 2 of this site's sourcing policy: no compound in this table has been the subject of a phase 2 or phase 3 RCT published in a major indexed journal with ED (Vesilut) at the bottom of that ranking with zero compound-specific studies. Second, the charge profiles differ meaningfully across the family — Vilon is near-neutral while Vesilut carries a double negative charge — which makes cross-compound extrapolation unreliable even as a rough guide. A researcher designing an assay for Vesilut should treat it as a structurally distinct probe, not as an interchangeable member of a homogeneous class.[1][2][3]
