What Prostamax Is
Prostamax is a synthetic tetrapeptide, Lys-Glu-Asp-Pro (KEDP), C20H33N5O9, 487.51 g/mol. Within the bioregulator family it is the prostate-associated member, and it is Vesugen's KED tripeptide extended by a proline.
Two published studies name it. Both are worth reading for what they are not: neither is a prostate study.
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 Two Studies Report
Heterochromatin in human lymphocytes
The primary paper examines the influence of the peptide bioregulator prostamax on heterochromatin of human lymphocytes in situ (Meskhi et al., Biofizika 2004, PMID 15612551).
This is a direct test of the family's central proposition — that short peptides act on chromatin — carried out in primary human cells rather than inferred from a downstream phenotype. It is the same experimental line as the Livagen chromatin work, and the two are best read together.
Microcalorimetry with metal ions
A second study used microcalorimetry on human blood lymphocyte cultures in the presence of copper, cadmium and prostamax (Kiladze et al., Georgian Med News 2009, PMID 19359734). The design is biophysical — it measures heat exchange in cell cultures — and the peptide appears alongside metal ions rather than as a sole intervention.
What the Prostate Label Rests On
Nothing in either paper concerns prostate tissue. The prostate association comes from the family's classification scheme, not from a published experiment on this sequence.
That does not make the label wrong; it makes it untested. If prostate activity is the research question, that gap belongs in the design rather than in the citation list.
Structure and Handling
- Sequence. Lys-Glu-Asp-Pro (KEDP), tetrapeptide.
- Formula. C20H33N5O9, 487.51 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
KEDP is KED plus proline. Vesilut (Glu-Asp) is a fragment contained within it. Pancragen (KED + Trp) has the family's largest literature. Full set on the bioregulator overview.
Research Studies at a Glance
The two indexed studies of Prostamax (KEDP) address distinct experimental questions and use different biophysical methods. Neither has been replicated by an independent group, and no dose-response or concentration data are reported in the publicly available abstracts. The table below summarises what the record actually contains; any cell marked "not reported" reflects an absence in the source, not an omission here.
| Study | Year | Model | Intervention / Design | Key Finding | PMID |
|---|---|---|---|---|---|
| Meskhi et al., Biofizika | 2004 | Human lymphocytes, in situ | KEDP applied to primary human lymphocyte cultures; heterochromatin assessed by unspecified cytological method | Reported influence on heterochromatin organisation; quantitative parameters not reported in abstract | [1] 15612551 |
| Kiladze et al., Georgian Med News | 2009 | Human blood lymphocyte cultures, in vitro | Microcalorimetry of cultures co-exposed to copper, cadmium, and KEDP; KEDP not tested as sole agent | Altered heat-exchange profiles in the presence of metal ions; peptide-specific contribution not isolated | [2] 19359734 |
Two design features constrain interpretation across both studies. First, the lymphocyte model was chosen to test the bioregulator family's chromatin hypothesis — it is not a prostate-relevant tissue. Second, the 2009 microcalorimetry study is a multi-agent design: because KEDP was not tested in isolation, any thermal signal attributed to it carries confounding from the metal-ion co-treatments. These are not disqualifying limitations; they define the questions that remain open for follow-up work.
Proposed Chromatin Interaction Mechanism
No published study has traced the intracellular signalling cascade downstream of KEDP in molecular detail. What follows is the mechanistic framework the Khavinson bioregulator programme uses to interpret the family's chromatin effects — classified here as proposed, because direct receptor identification and pathway mapping for KEDP specifically have not been reported.
The central proposition of the tetrapeptide bioregulator class is that short, charged peptides interact with nucleosomal DNA or histone tails through electrostatic and hydrogen-bond contacts, and that this interaction shifts the local equilibrium between euchromatin and heterochromatin. KEDP carries a net anionic character at physiological pH (lysine +1, glutamate −1, aspartate −1, proline neutral: net −1), which distinguishes it from the cationic peptides — such as protamines and certain histone N-terminal domains — that compact chromatin. A peptide with net negative charge at the concentrations used in cell-culture assays might instead compete with, or displace, endogenous anionic regulators at histone-binding sites. This is a plausible but unverified mechanism: it has not been tested with recombinant histones, and no binding constant for KEDP–nucleosome interaction has been published.[1]
The Meskhi et al. study[1] is consistent with a chromatin-accessibility effect, in that it reports a change in heterochromatin distribution in intact lymphocytes. However, the in situ design does not discriminate between a direct peptide–chromatin contact and an indirect route involving membrane receptors, second messengers, or altered transcription factor activity. All three pathways remain open hypotheses. Until binding assays with isolated chromatin components are published for KEDP specifically, the mechanism sits in the proposed register regardless of what has been demonstrated for the broader bioregulator family.
The co-exposure design of the Kiladze et al. study[2] raises a separate mechanistic question: whether KEDP modulates metal-ion uptake, chelates copper or cadmium extracellularly, or affects mitochondrial thermogenesis independently. The aspartate and glutamate residues confer weak metal-chelating potential, but no binding stoichiometry or affinity constant has been reported for KEDP with either ion. This, too, is an open experimental question rather than a settled finding.
Structural Comparison with Related Bioregulators
KEDP belongs to a family of short regulatory peptides developed within the same research programme. Comparing it structurally with its nearest relatives clarifies both what is shared across the family and what makes KEDP's sequence distinct. No head-to-head pharmacological comparison of these peptides has been published; the table below is therefore a structural comparison derived from sequence and formula data, not an efficacy comparison.
| Compound | Sequence | Length | Formula | MW (g/mol) | Net charge (pH 7.4, approx.) | Tissue label | Published human-cell chromatin data |
|---|---|---|---|---|---|---|---|
| Prostamax (KEDP) | Lys-Glu-Asp-Pro | 4-mer | C₂₀H₃₃N₅O₉ | 487.51 | −1 | Prostate (by classification) | Yes — Meskhi et al. 2004[1] |
| Vesugen (KED) | Lys-Glu-Asp | 3-mer | C₁₅H₂₆N₄O₈ | 394.39 | −1 | Vascular | Not identified in public record |
| Livagen (KHLGE) | Lys-His-Leu-Gly-Glu | 5-mer | C₂₄H₄₁N₇O₉ | 587.63 | ~0 to −1 | Lymphocyte / liver | Yes — independent chromatin studies referenced in existing Livagen literature |
| Epithalon (AEDG) | Ala-Glu-Asp-Gly | 4-mer | C₁₄H₂₀N₄O₁₀ | 390.33 | −2 | Pineal / telomere | Yes — telomerase activation reported in lymphocytes |
The most informative structural comparison is KEDP versus its tripeptide precursor KED (Vesugen). The C-terminal proline in KEDP introduces conformational rigidity — proline's pyrrolidine ring prevents rotation around the N–Cα bond — which restricts the backbone dihedral angles available to the tetrapeptide relative to the free tripeptide. Whether this conformational constraint changes chromatin-binding affinity, cellular uptake, or metabolic stability has not been tested for this pair specifically. It is a tractable experimental question: circular dichroism or NMR comparison of KED and KEDP in the presence of nucleosomal components would address it directly.
Epithalon (AEDG) is the only other 4-mer in this family with published human lymphocyte data and provides the clearest structural parallel, though the two sequences share no positional identity beyond the Glu-Asp dipeptide at positions 2–3 of Epithalon and positions 2–3 of Prostamax. The functional significance of that shared motif, if any, is not established.
