Prostamax (KEDP) Molecular Structure#

Sequence#

Prostamax is a linear synthetic tetrapeptide with the sequence:

• Three-letter code: Lys-Glu-Asp-Pro
• Single-letter code: KEDP
• Composition: L-lysine (basic), L-glutamic acid (acidic), L-aspartic acid (acidic), L-proline (cyclic, conformationally restricted)

The peptide carries a free N-terminal amine (on lysine) and a free C-terminal carboxylate (on proline), with two acidic side chains (Glu, Asp) and one basic side chain (Lys). Proline's pyrrolidine ring imposes a conformational restriction at the C-terminus that limits backbone flexibility.

Mass and Formula#

• Molecular weight: approximately 488 Da
• Molecular formula: C20H36N6O8 (free peptide; varies slightly for salt forms)
• CAS Registry Number: not assigned in the public literature reviewed

Structural Characterisation#

There is no published crystal structure, NMR ensemble, or cryo-EM model of Prostamax in the public structural databases. The Protein Data Bank (PDB) does not contain a KEDP entry. The peptide's three-dimensional behaviour has not been characterised in PubMed-indexed structural biology literature.

This is a notable gap, because the Khavinson bioregulator framework proposes that KEDP binds DNA in a sequence-specific manner. Demonstrating that mechanism rigorously would normally require:

• Crystal structure of the peptide-DNA complex
• Or solution NMR data on peptide-DNA interactions
• Or surface plasmon resonance / isothermal titration calorimetry data quantifying binding affinity and specificity
• Or independent biochemical evidence of sequence-selective binding

None of these has been published in PubMed-indexed form for Prostamax specifically.

Stability#

Stability data for Prostamax (lyophilised powder and reconstituted solution) are not available in PubMed-indexed literature. General short-peptide handling principles -- cold storage of the lyophilised form, refrigerated short-term storage of the reconstituted solution -- are typically applied by vendors but are not Prostamax-specific.

Relationship to Other Khavinson Short Peptides#

Prostamax shares the short, charged-residue-dominated architecture of other Khavinson bioregulators. The closest comparators are:

• Vesugen (Lys-Glu-Asp / KED): a tripeptide that shares the N-terminal Lys-Glu-Asp motif of Prostamax. Vesugen is proposed as a vascular-endothelial bioregulator.
• Vilon (Lys-Glu / KE): a dipeptide that shares the first two residues. Proposed as a thymus/immune bioregulator.
• Epitalon (Ala-Glu-Asp-Gly / AEDG): a tetrapeptide with different N- and C-termini. Proposed as a pineal bioregulator.

Within the Khavinson program, the variation in the C-terminal residue (proline in Prostamax, glycine in Epitalon, arginine in Pinealon, etc.) is proposed to confer tissue-specific gene-regulatory activity. The independent structural and biochemical evidence supporting this tissue-selectivity model is limited.

Related Reading#

• Prostamax research and evidence base
• Prostamax dosing protocols
• Vesugen molecular structure
• Epitalon molecular structure