KPV is a short anti-inflammatory peptide that is an active fragment of the alpha-melanocyte-stimulating hormone. It plays an important role in regulating inflammatory reactions, immune response, and tissue repair, especially of the skin, mucous membranes, and intestines. Due to its mild and physiological action, KPV is considered one of the basic peptide bioregulators of health, widely used in complex anti-age and longevity protocols.
For research purposes, KPV was studied for:
The KPV peptide sequence is a useful research tool for studying the regulation of innate immunity, mucosal protection, and new mechanisms of action of anti-inflammatory peptides.
General information
| Features | Values |
|---|---|
| The peptide sequence | Lys-Pro-Val (H-Lys-Pro-Val-OH) |
| The molecular formula | C16H30N4O4 |
| Molecular weight | 342.43 g/mol |
| CAS Number | 67727-97-3 |
| PubChem CID | 125672 |
| Synonyms | α-MSH(11-13), ACTH(11-13), MSH(11-13) |
Lyophilized peptides
All peptides undergo lyophilization, a process that is necessary to extend their shelf life, as well as preserve the purity and integrity of the peptides during storage and transportation. Product Usage: This product is intended solely for research purposes. All product information provided on this website is intended for educational purposes.
Product Usage
This product is intended solely for research purposes. All product information provided on this website is intended for educational purposes.
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KPV (Lys-Pro-Val) is a C-terminal tripeptide fragment of alpha-melanocyte-stimulating hormone (alpha-MSH, positions 11-13), which has been studied for its anti-inflammatory properties in the laboratory. Studies show that KPV acts through pathways independent of melanocortin receptors, which distinguishes it from the original molecule.
Molecular mechanisms
KPV penetrates cells through the PepT1 oligopeptide transporter with high affinity (Km ~160 µm in Caco2 cells). Studies show that the peptide accumulates in the nucleus for 5 hours, where it competitively disrupts the interaction between p65RelA and importin-α3, blocking the nuclear translocation of NFkB.
At nanomolar concentrations (10 nM), KPV also suppresses all three major MAPK subfamilies (ERK1/2, JNK, and p38) in intestinal epithelial cells. This mechanism acts independently of melanocortin receptors and reduces the expression of inflammatory cytokines.
Models of gastrointestinal tract inflammation
Oral administration of KPV in mouse models of colitis caused by DSS and TNBS demonstrated a significant reduction:
Studies show that the effectiveness of KPV correlates with the expression of PepT1, which increases in the inflamed epithelium of the colon and immune cells during IBD (inflammatory bowel disease).
Studies of the respiratory tract and lungs
In bronchial epithelial cells (16HBE14o-) KPV reduced inflammatory reactions caused by TNFa:
These results suggest potential applications in models of respiratory tract inflammation research.
Modulation of immune cells
Human Jurkat T cells and intestinal immune populations express functional PepT1, which allows KPV to absorb the drug. Studies show that 10 nM KPV stabilizes IkBa protein levels and reduces IL-8 transcription by about 40% after TNFa stimulation.
Under conditions of inflammation, PepT1 expression increases in macrophages of the intrinsic lamina of the mucous membrane and peripheral T cells, providing disease-activated delivery routes for peptide-based research tools.
Dermatological research
KPV retains its anti-inflammatory activity without activating MC1R, the melanogenesis receptor. This property makes it useful for studies of skin inflammation, where the effects of pigmentation can distort the results.
Stereoisomers such as KdPT (Lys-D-Pro-Thr) exhibit enhanced proteolytic stability. Studies on sebocytes have shown that KdPT suppresses IL-1b-mediated cytokine signaling, which is relevant for studies of the pathogenesis of acne.
The relationship between structure and activity
The KPV tripeptide is a minimal α-MSH sequence that retains anti-inflammatory activity. Studies with deletions confirm that truncating beyond KPV eliminates efficiency.
Substitutions with D-amino acids (KdPV, KPdV, dKPV) remain active, while increasing resistance to proteolysis. Glycoalkylation of the lysine residue increases stability, but eliminates antimicrobial properties, demonstrating structure-dependent profiles of biological activity.
For research purposes only: KPV is intended for in vitro laboratory studies and experimental protocols. All of these results are preclinical research models and have not been validated for therapeutic use.
Links
1. Dalmasso G, Charrier–Hisamuddin L, Thu Nguyen HT, Yan Y, Sitaraman S, Merlin D. PepT1-Mediated Tripeptide KPV Uptake Reduces Intestinal Inflammation. Elsevier BV; 2008. https://doi.org/10.1053/j.gastro.2007.10.026
2. Land S. Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. International Journal of Physiology, Pathophysiology and Pharmacology 2012;4 2:59–73.
3. Böhm M, Luger T. Are melanocortin peptides future therapeutics for cutaneous wound healing?. Wiley; 2019. https://doi.org/10.1111/exd.13887
4. Luger TA, Brzoska T. α-MSH related peptides: a new class of anti-inflammatory and immunomodulating drugs. Elsevier BV; 2007. https://doi.org/10.1136/ard.2007.079780
5. Songok AC, Panta P, Doerrler WT, Macnaughtan MA, Taylor CM. Structural modification of the tripeptide KPV by reductive “glycoalkylation” of the lysine residue. Public Library of Science (PLoS); 2018. https://doi.org/10.1371/journal.pone.0199686