KPV is a tripeptide consisting of lysine, proline, and valine — the C-terminal fragment of alpha-melanocyte-stimulating hormone (α-MSH). It is one of the smallest peptides in the research catalog, yet it retains the anti-inflammatory character associated with its parent sequence in model systems, which is why its simple chemistry attracts sustained interest.
A minimal active fragment
KPV represents the terminal three residues of the α-MSH sequence, and it is studied as the smallest portion still linked to the modulatory activity described in its mechanism of action. The broader concept of an active peptide fragment — how a short sequence can preserve behavior of a much larger molecule — is covered in understanding amino acid sequences.
Residue roles
The three residues each contribute distinct chemistry: lysine carries a basic, positively charged side chain; proline introduces a rigid ring that constrains the backbone conformation; and valine adds a small hydrophobic terminus. This compact mix of charge, rigidity, and hydrophobicity defines the fragment's physicochemical fingerprint.
Relationship to GHK-KPV
The same tripeptide appears fused to a copper-binding motif in GHK-KPV, illustrating how short, well-defined peptides are combined into hybrid research molecules that carry two motifs on a single chain.
Simple synthesis
As a three-residue peptide, KPV is quick and efficient to assemble by solid-phase synthesis, requiring only a handful of coupling and deprotection cycles. Its brevity means few deletion or truncation byproducts, which simplifies downstream purification.
Drying and QC
After cleavage and purification the peptide is lyophilized for stability (what is lyophilization) and then checked for identity and purity by HPLC and mass measurement. Broader context is in the KPV research overview.
Product page: KPV research vials.
Research Use Only. Supplied strictly for laboratory research and development — not for human or veterinary use, consumption, or any therapeutic or diagnostic purpose. This article is research education, not usage guidance.