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Peptide Library · Recovery & Repair
Tripeptide — C-terminal fragment of α-melanocyte-stimulating hormone

KPV

Also known as Lysine-Proline-Valine, α-MSH(11-13)

KPV is a three-residue peptide taken from the C-terminus of α-MSH. A research-use profile: its melanocortin origin, why the tripeptide is studied on its own, and how it's handled.

KPV is almost the smallest thing you can call a peptide and still have it be interesting — just three amino acids, lysine-proline-valine. What makes it worth a page is not its size but its pedigree: it is the tail end of α-melanocyte-stimulating hormone, clipped off and studied in isolation.

The account below sticks to what is established — its identity as an α-MSH fragment, the research areas the melanocortin literature places it in, and how it is handled in the lab. It avoids the language of outcomes and dosing entirely.

The sequence
3 residues · hover a position to read its amino acid

KPV is a tripeptide corresponding to the last three residues (positions 11–13) of α-melanocyte-stimulating hormone (α-MSH). It is one of the shortest peptides in the research catalog — three amino acids, no disulfide bonds.

A fragment of α-MSH

α-Melanocyte-stimulating hormone is a 13-residue peptide from the melanocortin family, itself derived from the larger precursor protein pro-opiomelanocortin (POMC). KPV corresponds to its final three residues — positions 11, 12, and 13. Written out, that is Lys-Pro-Val, the same three letters that give the peptide its name.

Isolating the C-terminal tripeptide is a deliberate research strategy: it separates a defined tail region from the parts of α-MSH that engage the classical pigmentation machinery, letting researchers study that short segment on its own terms. That is why KPV is discussed as an α-MSH fragment rather than as a melanocortin agonist in its own right.

Why a three-letter peptide gets studied at all

Short peptides are attractive to researchers precisely because they are simple: a defined, unambiguous sequence, no folding to worry about, and easy synthesis and characterization. KPV's tripeptide identity means a certificate of analysis should map cleanly onto a very small, well-defined mass — there is not much room for interpretation.

Its brevity is also why it is so frequently mentioned alongside other small recovery-context peptides like BPC-157 and GHK-Cu: these are all short, defined sequences studied in overlapping tissue and barrier research areas, and they are easy to group together for that reason.

Studied in the context of
Melanocortin-fragment researchEpithelial & barrier modelsInflammation-pathway researchGastrointestinal-lining studies

These are research areas the compound is associated with in the literature — not medical claims or intended uses.

Handling & storage

Supplied lyophilized. Stored sealed and cold; reconstituted with bacteriostatic water only when a protocol requires it, then kept refrigerated. As a very short peptide it is straightforward to characterize — handle per accepted laboratory practice.

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Common questions

What does the name KPV stand for?

It is simply the one-letter codes of its three amino acids: K (lysine), P (proline), V (valine). The peptide is Lys-Pro-Val.

How is KPV related to α-MSH?

KPV is the C-terminal tripeptide of α-melanocyte-stimulating hormone — residues 11 through 13. It is a fragment of that larger 13-residue melanocortin peptide.

Is KPV a melanocortin agonist like the full α-MSH molecule?

This page does not make functional claims. KPV is studied as an isolated C-terminal fragment, separated from the parts of α-MSH associated with classical pigment signaling; that separation is the reason researchers examine the tripeptide on its own.


View KPV in the catalog →Certificates of analysis
Related research
BPC-157GHK-CuLL-37Melanotan IIVIP
Reference

This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.