Vesugen (KED, T-38) Molecular Structure#

Sequence#

Vesugen is a linear synthetic tripeptide with the sequence:

• Three-letter code: Lys-Glu-Asp
• Single-letter code: KED
• Khavinson program designation: T-38
• Composition: L-lysine (basic), L-glutamic acid (acidic), L-aspartic acid (acidic)

The peptide carries a free N-terminal amine (on lysine) and a free C-terminal carboxylate (on aspartic acid), with one basic side chain (Lys, ε-amine) and two acidic side chains (Glu and Asp γ- and β-carboxylates). The peptide is highly polar.

Mass and Formula#

• Molecular weight: approximately 390.39 Da
• Molecular formula: C15H26N4O8 (free peptide; varies 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 Vesugen. The Protein Data Bank (PDB) does not contain a KED entry. The proposed three-dimensional behaviour rests on in-silico molecular docking predictions from Khavinson et al. 2021 (PMID 34071923), which modelled KED binding to promoter regions of AD-relevant genes (CASP3, NES, GAP43, APOE, SOD2, PPARA, PPARG)¹. Docking predictions are computational ranking exercises and require subsequent biophysical confirmation.

Direct biophysical confirmation of KED-DNA binding (NMR, surface plasmon resonance, isothermal titration calorimetry, or crystallography of the peptide-DNA complex) has not been published in PubMed-indexed form.

Stability#

Stability data for Vesugen are not available in PubMed-indexed literature. General short-peptide handling principles are applied by vendors:

• Cold storage of the lyophilised powder (2-8 C)
• Refrigerated short-term storage of reconstituted solution
• Protection from light and freeze-thaw cycles

These are general short-peptide conventions, not Vesugen-specific stability data.

Relationship to Other Khavinson Short Peptides#

Vesugen shares structural elements with the broader Khavinson family:

• Prostamax (KEDP, Lys-Glu-Asp-Pro): Vesugen is the N-terminal three residues of Prostamax
• Vilon (KE, Lys-Glu): Vesugen shares the first two residues with Vilon
• Pinealon (EDR, Glu-Asp-Arg): different sequence but co-tested with KED in PMID 34071923
• Epitalon (AEDG, Ala-Glu-Asp-Gly): different N- and C-termini, but shares the central acidic Glu-Asp pair

Within the Khavinson model, these short peptides are proposed to confer tissue-selective gene-regulatory activity based on the specific residue combination. Independent biophysical evidence supporting this claim is limited.

References#

Related Reading#

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

Footnotes#

1. Khavinson V, Ilina A, Kraskovskaya N, Linkova N, Kolchina N, Mironova E, Erofeev A, Petukhov M. Neuroprotective Effects of Tripeptides -- Epigenetic Regulators in Mouse Model of Alzheimer's Disease. Pharmaceuticals. 2021. PMID: 34071923. DOI: 10.3390/ph14060515. ↩