Anti-Inflammatory Research Peptide / Melanocortin-Derived Tripeptide
Molecular Structure
Structure Description
KPV is a linear tripeptide composed of lysine, proline, and valine (Lys-Pro-Val). It corresponds to the C-terminal three-amino-acid sequence of α-melanocyte-stimulating hormone (α-MSH 11–13). Its compact structure has made KPV useful in experimental investigations of melanocortin-derived peptide signaling and peptide structure-function relationships.
Peptide Transporter 1 (PepT1/SLC15A1); NF-κB and MAPK-associated inflammatory signaling pathways KPV has been experimentally demonstrated to undergo PepT1-mediated uptake in intestinal epithelial and immune-cell systems. Its downstream experimental effects include modulation of NF-κB and MAP kinase signaling.
Experimental Applications
Inflammatory signaling research
NF-κB pathway studies
MAP kinase pathway studies
Cytokine-expression research
PepT1 peptide-transport studies
Intestinal epithelial-cell research
Immune-cell signaling
Melanocortin-derived peptide research
Peptide uptake studies
Gastrointestinal experimental models
Peptide structure-function analysis
Experimental Systems
Published experimental systems involving KPV include:
Caco2-BBE human intestinal epithelial cells
HT29-Cl.19A intestinal epithelial cells
Jurkat human T cells
Human keratinocyte models
PepT1 transport systems
DSS-induced mouse colitis models
TNBS-induced mouse colitis models
CD45RB-high transfer colitis models
MC1R-deficient experimental models
These are published research systems and do not represent approved clinical applications
For the OPTMZ product itself, analytical endpoints include chromatographic purity, identity, KPV content, and endotoxin concentration.
Mechanism / Research Context
KPV is the C-terminal Lys-Pro-Val tripeptide of α-MSH. Experimental research has investigated its effects on inflammatory signaling while showing that its mechanism is not necessarily identical to that of the full α-MSH peptide.
In intestinal epithelial and immune-cell models, KPV has been shown experimentally to undergo transport through PepT1. Studies have examined subsequent changes in NF-κB and MAP kinase activation and pro-inflammatory cytokine expression.
Additional preclinical research suggests that some KPV-associated activity can occur independently of functional MC1R signaling, indicating that its experimental mechanism is more complex than direct classical melanocortin receptor agonism alone.
Evidence Level
The research supporting these applications consists predominantly of cellular, biochemical, and animal-model studies rather than established human clinical evidence.
Research References
Dalmasso G, et al. PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation. Gastroenterology. 2008;134(1):166–178. PMID: 18061177. DOI: 10.1053/j.gastro.2007.10.026. Maaser C, et al. Melanocortin-derived tripeptide KPV has anti-inflammatory potential in murine models of inflammatory bowel disease. Inflamm Bowel Dis. PMID: 18092346. DOI: 10.1002/ibd.20334. Brzoska T, et al. Review of α-MSH and related tripeptides, including KPV, their biochemical characteristics and experimental inflammatory research. PMID: 18612139.
Analytical Characterization
Independent analytical testing of OPTMZ Peptides KPV 10 mg, batch/lot 2026/02, by Krause Analytical reported:
Chromatographic Purity: 99.6%
KPV Content: 8.86 mg
Label Claim: 10 mg
Percent of Label: 88.6%
Identity: Mass spectral match confirmed
CAS Number: 112965-21-6
Analysis Method: HPLC-UV-MS
Endotoxins: <0.5 EU/mL
Endotoxin Method: USP <85>
Lab Number: 205091
Project: 145211
The COA states that values are reported per vial unless otherwise noted.
Research Classification: Anti-Inflammatory Research Peptide
Compound Type: Tripeptide
Amino Acid Sequence: Lys-Pro-Val (KPV)
Peptide Length: 3 amino acids
CAS Number: 112965-21-6
Purity: 99.6% chromatographic purity
Identity: Confirmed by mass spectral match
Measured Content: 8.86 mg
Percent of Label: 88.6%
Analysis Method: HPLC-UV-MS
Endotoxins: <0.5 EU/mL
Endotoxin Method: USP <85>
Batch/Lot: 2026/02
The CAS number, chromatographic purity, measured content, identity confirmation, and endotoxin result above come directly from the Krause Analytical COA for the tested OPTMZ sample.
Analytical & Testing
Each tested batch of KPV undergoes analytical evaluation to verify chromatographic purity, identity, peptide content, and analytical consistency. A corresponding Certificate of Analysis is maintained for the tested lot.
For the submitted OPTMZ Peptides sample, independent testing by Krause Analytical reported:
Chromatographic Purity: 99.6%
Identity: Confirmed by mass spectral match
Measured Content: 8.86 mg
Label Claim: 10 mg
Percent of Label: 88.6%
Testing Method: HPLC-UV-MS
Endotoxins: <0.5 EU/mL
Endotoxin Method: USP <85>
CAS Number: 112965-21-6
Batch/Lot: 2026/02
The laboratory specifies that all values are reported on a per-vial basis unless otherwise noted.
The accompanying COA also includes the underlying chromatogram on page 2, which shows a dominant principal peak, and the mass-spectral report on page 3 supporting the identity analysis.
Handling & Storage
KPV should be handled by qualified professionals in controlled laboratory environments. Appropriate storage conditions should be maintained to preserve peptide stability and structural integrity.
Avoid unnecessary exposure to heat, moisture, and repeated temperature fluctuations. Experimental preparation, storage, and handling should follow validated laboratory procedures appropriate to the intended research application.
Research Context
KPV has been investigated in experimental systems involving inflammatory signaling, intestinal epithelial biology, immune-cell signaling, and melanocortin-derived peptide biology.
Research areas include:
NF-κB signaling
MAP kinase signaling
Pro-inflammatory cytokine expression
PepT1-mediated peptide transport
Intestinal epithelial-cell biology
Immune-cell signaling
Inflammatory pathway research
α-MSH-derived peptide biology
Cellular peptide uptake
Gastrointestinal experimental models
Peptide structure-function relationships
A published study using human intestinal epithelial cells and Jurkat T cells found KPV uptake was associated with PepT1 and examined NF-κB, MAP kinase pathways, and pro-inflammatory cytokine secretion. The same study also evaluated KPV in DSS- and TNBS-induced mouse colitis models.
Other experimental research has examined KPV in DSS and CD45RB-high transfer models of intestinal inflammation and reported that some observed activity persisted in mice with nonfunctional MC1R, suggesting that KPV’s experimental signaling cannot simply be attributed to conventional MC1R activation.
These findings describe preclinical experimental research and do not establish therapeutic efficacy or safety in humans.
Research Application Scope
KPV continues to be evaluated as an experimental research peptide for investigating inflammatory signaling, intestinal peptide transport, epithelial-cell responses, immune-cell biology, and molecular pathways associated with α-MSH-derived peptides.
Its three-amino-acid Lys-Pro-Val structure represents the C-terminal tripeptide of α-MSH. Despite lacking much of the parent peptide’s structure, KPV has retained biological activity in multiple experimental inflammatory models, making it useful for investigating structure-function relationships among melanocortin-derived peptides.
Use Statement
For laboratory research use only. Intended strictly for in vitro and controlled experimental research applications.
Disclaimer
All products currently listed on this site are for research purposes ONLY.
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