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Compound monograph

KPV

KPV is a synthetic tripeptide, Lys-Pro-Val, corresponding to the C-terminal three residues of alpha-melanocyte-stimulating hormone.

Published: 2026-09-12Literature/identifier verification: 2026-08-23
Lys-Pro-Valalpha-MSH (11-13)MSH (11-13)Melanocortin fragment peptides

01

Identity & nomenclature

KPV is a synthetic tripeptide, Lys-Pro-Val, corresponding to the C-terminal three residues of alpha-melanocyte-stimulating hormone.

KPV is the C-terminal tripeptide of alpha-melanocyte-stimulating hormone, residues 11 to 13, and is written in the literature as alpha-MSH(11-13). No UNII appears in a valid ten-character form in the PubChem synonym set for this record, so none is published here.

Declared aliases and development codes: Lys-Pro-Val, alpha-MSH (11-13), MSH (11-13).

02

Molecular properties

Molecular formulaC16H30N4O4
Molecular mass342.43 Da
CAS Registry Number67727-97-3
PubChem CID125672
One-letter sequenceKPV
Three-letter sequenceLys–Pro–Val

Tripeptide Lys-Pro-Val, corresponding to residues 11 to 13 of alpha-melanocyte-stimulating hormone. The correspondence is stated in the PubChem synonym record and in the source literature.

03

Structural characteristics

Structure-activity work on acetylated, amidated analogs of the alpha-MSH(11-13) sequence reports that substituting D-amino acids at each position affects activity differently: the L-configuration of the proline at position 12 was required, the L-configuration of the lysine at position 11 was not, and D-valine substitution at position 13 was reported to increase activity approximately fourfold relative to the all-L peptide. The source literature also reports that the tripeptide is associated with inhibition of NF-kappa-B activation through preservation of the inhibitory protein I-kappa-B-alpha.

04

Molecular targets & mechanisms

05

Analytical considerations

At 342 Da this is among the smallest peptides in the library. The sequence contains no aromatic residues and no sulfur, so UV detection at 280 nm gives no useful chromophore response and sulfur-based oxidation pathways do not apply. Because commercially supplied material may be acetylated at the N-terminus and amidated at the C-terminus, identity methods must establish which form is present.

06

Verified bibliography

  1. Anti-inflammatory activity of alpha-MSH(11-13) analogs: influences of alteration in stereochemistry.

    Hiltz ME, Catania A, Lipton JM

    Peptides · 1991-07 · Journal Article

    current
  2. The neuroimmunomodulatory peptide alpha-MSH.

    Ichiyama T, Sato S, Okada K, Catania A, Lipton JM

    Annals of the New York Academy of Sciences · 2000 · Review

    current
  3. Dissection of the anti-inflammatory effect of the core and C-terminal (KPV) alpha-melanocyte-stimulating hormone peptides.

    Getting SJ, Schiöth HB, Perretti M

    The Journal of pharmacology and experimental therapeutics · 2003-05-15 · Journal Article

    current

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

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