KPV Peptide – Anti-Inflammatory Tripeptide for Research Use Only

Introduction

The process of inflammation is complex and, in many cases, chronic. Under normal conditions, it protects tissues against trauma and infection, but if left unchecked, it can become a devastating force that promotes disease, damages organs, and harms overall health.

Identifying molecules capable of regulating inflammatory processes can be a game-changer for researchers seeking to understand and control these biological mechanisms.

KPV is a small yet powerful peptide rapidly gaining attention in inflammation research. It has shown the ability to regulate immune responses without systemic interactions, making it a fascinating subject of study.

KPV peptides available from Atlas Lab are intended for research and educational purposes only.

What Is KPV?

KPV is a naturally occurring tripeptide composed of three amino acids — Lysine, Proline, and Valine (Lys-Pro-Val).
It is a fragment of the larger peptide alpha-melanocyte-stimulating hormone (α-MSH), forming the C-terminal end of its 13-amino-acid sequence.

KPV replicates some biological activities of its parent peptide, particularly the anti-inflammatory actions mediated through melanocortin receptors (MCRs).

Because of its small molecular size, KPV is easily absorbed into cells via the proton-coupled oligopeptide transporter (PEP1), allowing for intracellular activity. Its simplicity also makes it easy to synthesize and modify compared to larger peptides.

Mechanism of Action

The inhibition of the nuclear factor kappa B (NF-κB) signaling pathway forms the foundation of KPV’s anti-inflammatory process.
NF-κB regulates pro-inflammatory gene expression, and studies show that KPV suppresses its activity by stabilizing the inhibitor protein IkB-alpha, preventing phosphorylation and degradation.

This, in turn, blocks the nuclear translocation of the p65ReIA subunit of NF-κB, resulting in reduced transcription of inflammatory cytokines such as TNF-α and IL-8.

Animal studies have demonstrated that KPV administration reduces neutrophil infiltration, cytokine levels, and MMP release, leading to decreased tissue inflammation and damage.
Importantly, KPV’s action is receptor-independent, distinguishing it from full α-MSH peptides and expanding its potential use in low-receptor-expression models.

A 2017 study in mice found that TNF-α was significantly downregulated after KPV treatment, further supporting its anti-inflammatory potential through the NF-κB pathway.

Research Applications of KPV

KPV peptides are primarily used to study the following mechanisms:

• Immune modulation
• Inflammation resolution
• Tissue repair

Because of its strong anti-inflammatory properties, KPV is valuable in research involving chronic inflammatory conditions such as:

• Inflammatory Bowel Disease (IBD)
• Acute Lung Injury
• Other epithelial tissue disorders

KPV studies help explain pathways that control:

• Pro-inflammatory cytokine regulation
• Immune cell infiltration
• Reparative processes in preclinical models

KPV is also used as a molecular probe in research to dissect signaling pathways, including NF-κB.
Common applications include:

• In vitro cell culture experiments
• Ex vivo tissue models
• In vivo rodent studies

These investigations contribute to a better understanding of KPV’s anti-inflammatory effects and its role in maintaining immune homeostasis.

Quality Control and Testing

Maintaining peptide quality is essential for accurate and reproducible results in KPV research.
Quality control procedures focus on accurate synthesis, purity verification, structural confirmation, and contaminant testing.

Table 1: Quality Control and Testing Process for KPV

Conclusion

KPV is a promising research peptide with targeted anti-inflammatory properties derived from the α-MSH C-terminal motif.
Its clear mechanism of action and receptor-independent effects make it ideal for studying inflammation, tissue repair, and immune modulation.

Maintaining strict quality standards ensures reliable and reproducible experimental outcomes.

KPV peptides provided by Atlas Lab are for research use only. They are not intended for diagnostic, therapeutic, or human applications.

Atlas Lab ensures top-tier quality assurance with verified Certificates of Analysis (COA) and the latest research updates to support inflammation and immune signaling studies with confidence.

References

1. Dall’Olmo, L., et al. Alpha-melanocyte stimulating hormone (α-MSH): biology, clinical relevance and implication in melanoma. Journal of Translational Medicine, 2023, 21(1): 562.
2. Yang, Y., et al. Amino acid residue L112 in the ACTH receptor plays a key role in ACTH or α-MSH selectivity. Molecular and Cellular Endocrinology, 2019, 482: 11–17.
3. Land, S.C. Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides. Int. J. Physiol. Pathophysiol. Pharmacol., 2012, 4(2): 59.
4. Songok, A.C., et al. Structural modification of the tripeptide KPV by reductive “glycoalkylation” of the lysine residue. PLOS ONE, 2018, 13(6): e0199686.
5. Killer, M., et al. Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes. Science Advances, 2021(7): eabk3259.
6. Pawar, K., et al. Transdermal iontophoretic delivery of lysine-proline-valine (KPV) peptide across microporated human skin. J. Pharm. Sci., 2017, 106(7): 1814–1820.
7. Benita, B.A., & Koss, K.M. Peptide discovery across the spectrum of neuroinflammation; microglia and astrocyte phenotypical targeting. Front. Mol. Neurosci., 2024, 17: 1443985.
8. Sung, J., et al. Lysine-Proline-Valine peptide mitigates fine dust-induced keratinocyte apoptosis and inflammation by regulating oxidative stress and modulating the MAPK/NF-κB pathway. Tissue and Cell, 2025, 95: 102837.
9. Xiao, B., et al. Orally targeted delivery of tripeptide KPV via hyaluronic acid-functionalized nanoparticles efficiently alleviates ulcerative colitis. Molecular Therapy, 2017, 25(7): 1628–1640.
10. Chen, W., et al. Optimization of a peptide extraction and LC–MS protocol for quantitative analysis of antimicrobial peptides. Future Science OA, 2019, 5(1): FSO348.
11. Fang, P., et al. Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptide analysis: Current state and new applications. Heliyon, 2024, 10(7).
12. Chen, L. & Mozier, N. Comparison of Limulus amebocyte lysate test methods for endotoxin measurement in protein solutions. J. Pharm. Biomed. Anal., 2013, 80: 180–185.

Shafi Ahman