KPV is a tripeptide composed of three amino acids (L-lysine, L-proline, L-valine) joined by two peptide bonds. It is the C-terminal tripeptide of the parent neuropeptide α-melanocyte-stimulating hormone (α-MSH). The peptide came to research attention through work characterizing its anti-inflammatory activity in multiple animal-model systems despite its lack of the residues required for activation of the classical melanocortin receptors.

How is KPV related to α-MSH?

KPV (Lys-Pro-Val) consists of the C-terminal three residues (positions 11-13) of the 13-residue α-MSH peptide. The parent α-MSH has the sequence Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2 and contains both the MSH 'core' sequence (His-Phe-Arg-Trp, positions 6-9) required for melanocortin-receptor activation and the C-terminal KPV that is proposed to mediate anti-inflammatory effects through different mechanisms.

The molecular mechanism of KPV's proposed anti-inflammatory activity has not been definitively established. The central hypothesis in the published literature is that the C-terminal tripeptide retains anti-inflammatory activity through mechanisms independent of activation of the five classical melanocortin receptors (which is precluded by the absence of the MSH core sequence). Proposed downstream mechanisms include effects on NF-κB signaling, mast-cell stabilization, modulation of cytokine production by various immune cell types, and effects on epithelial-barrier function in mucosal contexts. The specific molecular target(s) responsible remain one of the open questions of the field.

What does the published research describe?

The published KPV research literature describes anti-inflammatory effects characterized in multiple animal-model systems: intestinal-inflammation models (particularly dextran-sulfate-sodium and trinitrobenzenesulfonic-acid colitis), dermal-inflammation models (contact-hypersensitivity), mast-cell-mediated inflammation models, and broader characterizations of effects on cytokine production and inflammation-related gene expression. The mucosal- and intestinal-research context, particularly through the work of Didier Merlin's group at Emory, has been one of the most actively developed sub-areas.

Does KPV activate melanocortin receptors?

No, not in any meaningful way. The activation of MC1R through MC5R requires the MSH core sequence (His-Phe-Arg-Trp) that is present in the parent α-MSH but absent from the C-terminal KPV tripeptide. The published research literature has used the absence of meaningful melanocortin-receptor activation by KPV as one of the basis points for the hypothesis that KPV's anti-inflammatory effects operate through receptor-independent mechanisms.

Is KPV the same as the C-terminal of α-MSH?

Yes — KPV consists of the C-terminal three residues of α-MSH (positions 11-13). In the parent α-MSH the C-terminus is amidated, so the amide form (KPV-NH2) most closely corresponds to the native α-MSH C-terminal sequence. Research-peptide preparations may be supplied as either the free-acid form or the amide form, and this detail should be confirmed against the specific Certificate of Analysis for any given lot.

What is the molecular weight of KPV?

KPV (free-acid form, Lys-Pro-Val) has a molecular formula of C16H31N5O4 and a molecular weight of approximately 357.4 daltons. The C-terminal amide form (KPV-NH2, more closely corresponding to the native α-MSH C-terminus) has the formula C16H32N6O3 and a molecular weight of approximately 356.5 daltons. The molecular weight is among the smallest of the peptides discussed in this catalog, reflecting the tripeptide structure.

Is KPV approved as a medicine?

No. KPV is not approved as a medicine or as an anti-inflammatory therapy in the United States, the European Union, or other major regulatory jurisdictions. The compound has been characterized extensively in animal-model and preclinical research contexts, but it has not been advanced through pharmaceutical approval in any major regulatory context. The research-peptide form is supplied for laboratory and analytical use only.

What is the relationship to inflammatory bowel disease research?

The intestinal-inflammation research context for KPV, particularly developed through the work of Didier Merlin's group at Emory University, has framed continuing interest in the peptide as a tool for characterizing inflammatory-bowel-disease-related biology. Published studies in DSS and TNBS colitis models have characterized effects on histological inflammation, mucosal cytokine production, and epithelial-barrier function. Educational discussion of these research findings should remain within the laboratory/preclinical framing; KPV is not an approved IBD therapy.

What is the role of mast-cell stabilization?

Some published research has characterized KPV as a mast-cell stabilizer, with effects on histamine and other mediator release from mast cells in various experimental contexts. Mast cells play important roles in allergic inflammation, urticaria, and other mast-cell-driven inflammatory processes. The mast-cell-stabilizing characterization of KPV is one of several mechanism domains in the published research literature and contributes to the broader anti-inflammatory profile characterized in the laboratory studies.

How is KPV manufactured?

Research-grade KPV is produced by standard solid-phase peptide synthesis using Fmoc protecting-group chemistry. The short tripeptide sequence is straightforward to synthesize and presents no significant synthesis challenges. The C-terminal amide form (KPV-NH2) is synthesized on a Rink amide resin; the free-acid form is synthesized on a standard acid-functionalized resin. The crude peptide is purified by reversed-phase HPLC and characterized by mass spectrometry. Reputable suppliers report purity in the 98-99% range for research-grade material.

What storage practices apply?

Lyophilized KPV stored sealed at -20 °C or below away from light and moisture is generally considered stable for extended periods. The peptide has no methionine, no cysteine, and no aromatic residues — the most chemically vulnerable amino acid side chains — so it is relatively stable compared to many other research peptides. Reconstituted material in sterile aqueous solvent is typically held cold and used within weeks to months depending on the specific research application.

Why is KPV's mechanism described as 'receptor-independent'?

The 'receptor-independent' framing in the KPV literature specifically refers to independence from the classical melanocortin receptors (MC1R through MC5R), activation of which requires the MSH core sequence absent from KPV. The framing does not mean that KPV acts without any molecular target — the peptide presumably does interact with some molecular target(s) to produce its observed cellular effects on NF-κB signaling, mast-cell function, and epithelial-barrier biology. The specific molecular target(s) have not been definitively identified, and the term 'receptor-independent' is shorthand for 'independent of the classical melanocortin GPCRs.'

How does KPV differ from α-MSH?

α-MSH is a 13-residue neuropeptide (Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2) with full activity at melanocortin receptors MC1R through MC5R, mediating effects on pigmentation, energy balance, sexual function, and inflammation. KPV is the C-terminal tripeptide (Lys-Pro-Val) of α-MSH with substantially smaller molecular size, no meaningful melanocortin-receptor activity, and a research focus narrowly on the anti-inflammatory effects. The dissociation between the receptor-mediated effects of the parent α-MSH and the receptor-independent anti-inflammatory effects of the C-terminal KPV is one of the central themes that motivates KPV research.

What about oral KPV in research contexts?

Oral administration of unmodified KPV is limited by gastric and intestinal proteolytic degradation, which limits the systemic bioavailability of the intact peptide following oral dosing. In animal-model research contexts, KPV has been administered through various routes including intraperitoneal, intravenous, and (notably for intestinal-inflammation models) intracolonic administration. Some research has explored modified KPV analogs and various formulation approaches to improve oral or topical bioavailability for specific experimental applications.

What does KPV have to do with α-MSH agonists like Melanotan-2?

Melanotan-2 (MT-2) is a synthetic cyclic α-MSH analog designed for high-potency activation of melanocortin receptors (particularly MC1R for pigmentation and MC3R/MC4R for the central nervous system effects). MT-2 represents one direction of α-MSH structure-activity research — engineering for receptor potency — while KPV represents the opposite direction — characterizing the C-terminal fragment for receptor-independent effects. The two compounds are derived from the same parent α-MSH but occupy very different positions in the research-peptide landscape.

How does KPV compare to BPC-157?

Both are small peptides studied in animal-model contexts for anti-inflammatory and tissue-related effects, particularly in mucosal and gastrointestinal contexts. The two peptides are otherwise quite different — BPC-157 is a 15-residue pentadecapeptide derived from a stomach-juice protein, with proposed mechanisms centering on angiogenesis, growth-factor signaling, and broad tissue-healing effects; KPV is a 3-residue tripeptide derived from α-MSH, with proposed mechanisms centering on receptor-independent modulation of inflammatory signaling. Both have been studied in colitis models, providing one specific comparison point in the published literature.

KPV 10mg (with Bacteriostatic Water) lyophilized vial with bacteriostatic water for research

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KPV 10mg (with Bacteriostatic Water)

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KPV (Lysine-Proline-Valine) is a naturally derived tripeptide fragment studied in immunology, inflammation biology, and gastrointestinal research. It is a C-terminal fragment of the alpha-melanocyte stimulating hormone (α-MSH) pathway and has gained attention in preclinical studies for its role in inflammatory signaling modulation and epithelial barrier research. This compound is manufactured to strict laboratory-grade standards and is intended strictly for qualified scientific and preclinical research use only.

KPVLys-Pro-ValAnti-Inflammatoryα-MSH FragmentTripeptideLyophilized

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