KPV 10 mg

KPV — 10 mg

Purity: ≥98% (HPLC)
Form: lyophilized powder, 3 mL vial
Storage: −20 °C (before opening), +2…+8 °C (after reconstitution, no more than 28 days)
Verification: Janoshik Analytical (Czech Republic) — independent blind test of each batch
Synonyms: KPV, Lys-Pro-Val, α-MSH (11-13), C-terminal tripeptide of alpha-MSH

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Contents

1. What is KPV?
2. Why KPV attracts researchers' attention
3. Peptide structure
4. NF-κB — in simple terms
5. KPV and the PepT1 transporter
6. Studies in models of intestinal inflammation
7. KPV in dermatological research
8. KPV in combination with other peptides
9. Sources

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1. What is KPV?

KPV is one of the smallest biologically active peptides known to science. Just three amino acids: lysine, proline, valine. It is the C-terminal fragment of α-MSH (alpha-melanocyte-stimulating hormone) — positions 11, 12 and 13 in its 13-amino-acid chain.

In 1989, Hiltz and Lipton showed that this tiny fragment retains a significant portion of the anti-inflammatory activity of full-length α-MSH, while being entirely devoid of its pigmenting and hormonal action. This discovery made KPV an independent object of research.

Since then, KPV has been studied in the context of inflammatory processes of the intestine, the skin, and immune regulation. Its main mechanism is suppression of the NF-κB signaling pathway, one of the principal "conductors" of inflammation in the body.

For research use only. Not a medicinal product. Not intended for use in humans or animals.

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2. Why KPV attracts researchers' attention

KPV is of interest for several reasons, each of which is supported by publications:

• Minimal size — maximal activity. Three amino acids — yet it reproduces much of the anti-inflammatory effect of the 13-amino-acid hormone. Luger and Brzoska state directly: most of the anti-inflammatory activity of α-MSH is localized precisely in the C-terminal tripeptide KPV [1].

• Works without receptors. Unlike full-length α-MSH, KPV does not bind to the melanocortin receptors on the cell surface. It penetrates inside the cell and acts directly on intracellular signaling cascades [2][3]. This means: no effect on pigmentation and no hormonal effects.

• A unique delivery route. KPV is transported into intestinal epithelial cells through the PepT1 transporter — the very one that normally carries di- and tripeptides from food [4]. This mechanism is described as potentially significant for delivering the peptide directly to inflamed tissue.

• Suppression of NF-κB by up to 80%. In some experimental models, a reduction in nuclear translocation of NF-κB — the central regulator of inflammatory genes — of up to 80% was observed [4].

All of the data listed were obtained under laboratory conditions (in vitro) and in animal models. No clinical studies in humans have been conducted.

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3. Peptide structure

Parameter	Value
Amino acid sequence	Lys-Pro-Val
Molecular formula	C₁₆H₃₀N₄O₄
Molecular weight	342.43 g/mol
CAS number	65189-71-1
Origin	C-terminal fragment of α-MSH (positions 11–13)
Type	Natural tripeptide
Receptor activity	Does not bind to melanocortin receptors
Transport	Via PepT1 (oligopeptide transporter)

KPV is, in essence, the "address" of the anti-inflammatory signal within the α-MSH molecule. The full-length hormone carries both an anti-inflammatory function and a pigmenting one (via melanocortin receptors). In KPV, only the former is preserved.

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4. NF-κB — in simple terms

To understand how KPV works, one needs to understand its target.

NF-κB (nuclear factor kappa-B) is a protein that can be called the "master switch of inflammation." When a cell receives a danger signal (infection, injury, stress), NF-κB is activated, moves into the cell nucleus, and "switches on" hundreds of genes responsible for the inflammatory response: production of cytokines (TNF-α, IL-1β, IL-6, IL-8), recruitment of immune cells, intensification of edema.

Under normal conditions this is a protective reaction. But when NF-κB becomes "stuck" in the active state, inflammation becomes chronic — and begins to destroy the body's own tissues. It is precisely this scenario that is studied in the context of inflammatory bowel diseases, skin inflammation, and autoimmune conditions.

In experimental models, KPV suppresses the activation of NF-κB and reduces the MAPK (mitogen-activated protein kinase) cascade — another key signaling pathway of inflammation [2][4]. The result: in experiments, a reduction in the production of pro-inflammatory cytokines — TNF-α, IL-1β, IL-6, IL-8 — was observed.

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5. KPV and the PepT1 transporter

One of the most interesting features of KPV is the way in which it gets inside the cell.

PepT1 (SLC15A1) is a transporter embedded in the membrane of intestinal epithelial cells. Its usual job is to carry di- and tripeptides from digested food into the cell. KPV, being a tripeptide, uses precisely this transporter.

In 2008, the Dalmasso group showed that KPV penetrates intestinal epithelial cells and immune cells (T lymphocytes) through PepT1 [4]. Moreover, the expression of PepT1 increases during intestinal inflammation. This creates a kind of "targeted delivery": the stronger the inflammation, the more transporter on the membrane, and the more KPV gets inside the cell.

It is precisely this mechanism that makes KPV a subject of interest in research related to inflammatory processes in the gastrointestinal tract.

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6. Studies in models of intestinal inflammation

Key study: Dalmasso et al. (2008), published in a peer-reviewed journal [4].

The experiments used:

• Intestinal epithelial cell cultures (Caco2-BBE, HT29-Cl.19A)
• T lymphocytes (Jurkat)
• Two mouse models of colitis (DSS and TNBS)

Results:

• At nanomolar concentrations, KPV suppressed the activation of NF-κB and MAPK
• It reduced the secretion of pro-inflammatory cytokines
• When added to the drinking water of mice, a reduction in the manifestations of DSS- and TNBS-induced colitis was observed
• The effect was PepT1-dependent — when the transporter was blocked, the anti-inflammatory action weakened

The authors note that KPV may be considered a potential object for further research in the field of inflammatory bowel diseases.

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7. KPV in dermatological research

In addition to the intestine, KPV is studied in the context of inflammatory processes of the skin.

In a 2019 review, Luger and Böhm analyze the prospects of melanocortin peptides, including KPV, in wound-healing research [5]. In earlier work, Elliott et al. (2004) described the signaling pathways of KPV in keratinocytes — the main cells of the epidermis [6].

Directions of KPV dermatological research:

• Contact dermatitis — in models, a reduction in hypersensitivity was observed [3]
• Wound healing — suppression of excessive inflammation may contribute to cleaner tissue restoration
• Oxidative stress of keratinocytes — a protective action of KPV under the influence of external factors has been described [7]

All data are preclinical. No large-scale studies in humans in the dermatological context have been conducted.

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8. KPV in combination with other peptides

KPV is often mentioned in the research literature in the context of combinations with other peptides, where each component acts on its own mechanism:

Component	Mechanism	Focus
KPV	Suppression of NF-κB, reduction of cytokines	Anti-inflammation
BPC-157	Angiogenesis (vessel growth), fibroblast migration	Tissue restoration
TB-500	Migration of cells to the site of injury	Systemic restoration
GHK-Cu	Synthesis of collagen and elastin	Skin renewal

In the LONGIVIYA catalog, the combination of all four is presented as Blend Premium (80 mg) — for research protocols that combine anti-inflammatory and restorative approaches.

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Sources

1. Luger T.A., Brzoska T. Alpha-MSH related peptides: a new class of anti-inflammatory and immunomodulating drugs. Ann. Rheum. Dis., 66(Suppl 3): iii52–iii55, 2007. PubMed

2. Getting S.J. et al. Dissection of the anti-inflammatory effect of the core and C-terminal (KPV) alpha-melanocyte-stimulating hormone peptides. J. Pharmacol. Exp. Ther., 306(2): 631–637, 2003. PubMed

3. Brzoska T. et al. Alpha-melanocyte-stimulating hormone and related tripeptides: biochemistry, anti-inflammatory and protective effects in vitro and in vivo, and future perspectives. Endocr. Rev., 29(5): 581–602, 2008. PubMed

4. Dalmasso G. et al. PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation. Gastroenterology, 134(1): 166–178, 2008. PubMed

5. Luger T.A., Böhm M. Are melanocortin peptides future therapeutics for cutaneous wound healing? Exp. Dermatol., 28(8): 900–905, 2019.

6. Elliott R.J. et al. Alpha-melanocyte-stimulating hormone, MSH 11-13 KPV and adrenocorticotropic hormone signalling in human keratinocyte cells. J. Invest. Dermatol., 122(4): 1010–1019, 2004.

7. Brzoska T. et al. Terminal signal: anti-inflammatory effects of α-melanocyte-stimulating hormone related peptides beyond the pharmacophore. Adv. Exp. Med. Biol., 681: 107–116, 2010. PubMed

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This material was prepared by the LONGIVIYA editorial team on the basis of published scientific research. The information is for educational purposes only and is not a medical recommendation.

For research use only. Not a medicinal product. Not intended for use in humans or animals. Independent verification of each batch: Janoshik Analytical (Czech Republic).