KPV
KPV is the tripeptide lysine-proline-valine, the C-terminal sequence of alpha-melanocyte-stimulating hormone. It is studied for anti-inflammatory effects in cell and rodent models, particularly of intestinal inflammation, and is not approved for any use.
Most published evidence on KPV comes from animal and cell studies. Findings in those models have not been established in people.
Overview
KPV is a three-residue peptide corresponding to the C-terminal end (residues 11–13) of alpha-melanocyte-stimulating hormone (α-MSH), a peptide derived from proopiomelanocortin. α-MSH has well-documented anti-inflammatory activity in experimental systems, and early work suggested that part of this activity could be reproduced by its C-terminal tripeptide, which lacks the core sequence associated with pigmentation. This made KPV an attractive candidate for studying anti-inflammatory signaling separately from melanocortin effects on skin color, and it has since been examined as a minimal active fragment in its own right.
Research on KPV has focused on inflammation of the intestine and skin. Cell studies have examined inflammatory signaling in epithelial and immune cells, and rodent studies have tested KPV in models of colitis, often using oral or nanoparticle-based delivery. There are no published controlled clinical trials establishing effects in people, and the compound remains a preclinical research peptide. Most published studies come from a small number of research groups, and comparisons between them are complicated by differences in peptide form and delivery system.
Structure
KPV is the linear tripeptide Lys-Pro-Val. It appears in the literature both as a free acid and as a C-terminal amide (KPV-NH2), mirroring the amidated C-terminus of native α-MSH, and these forms should not be treated as interchangeable. Analogues with D-amino acids have also been studied. KPV contains no oxidation-prone residues. Its small size and basic lysine side chain mean that counter-ions such as acetate or TFA can account for a large fraction of the powder mass.
Mechanism
Proposed mechanisms come from in-vitro and rodent studies. KPV has been reported to reduce activation of NF-κB and MAPK inflammatory pathways and lower production of pro-inflammatory cytokines in intestinal epithelial and immune cells. In intestinal cells, uptake through the di- and tripeptide transporter PepT1 has been described as one route by which KPV enters cells and acts intracellularly. Whether KPV acts through melanocortin receptors, as α-MSH does, is debated; some studies suggest receptor-independent effects. These mechanisms have not been confirmed in humans.
Research
Intestinal inflammation models
The most cited KPV research uses mouse models of chemically induced colitis. Authors have reported reduced inflammatory markers and tissue damage in treated animals, and have linked the effects to PepT1-mediated uptake in intestinal epithelium. Later studies explored oral delivery using nanoparticles or hydrogels designed to release the peptide in the colon. These findings are preclinical and have not been tested in controlled human trials.
Skin and wound models
As a fragment of α-MSH, KPV has been investigated in skin-inflammation and wound models in cells and animals, with reports of reduced inflammatory signaling. Some work has examined its incorporation into topical or biomaterial formulations. The volume of evidence is small, and results come from experimental models only. Human skin data are lacking, and the relationship between KPV and the broader activity of α-MSH in skin has not been clearly defined.
Antimicrobial activity
Some in-vitro studies of α-MSH and its C-terminal fragments have reported activity against certain microbes, including Candida albicans and Staphylococcus aureus. This line of work is limited, and it is unclear whether such activity occurs at relevant concentrations in living tissue. It should be regarded as exploratory. Most reports involve simple in-vitro susceptibility assays, and in-vivo infection models are scarce.
Evidence quality
KPV has a coherent but narrow preclinical evidence base centered on intestinal inflammation in rodents. There are no published randomized controlled trials in people, and safety in humans has not been systematically studied. Differences between free-acid and amidated forms, and between delivery systems, complicate comparison across studies. Independent replication across laboratories is also limited, and long-term safety data are absent.
Regulatory status
KPV is not approved by the FDA for any use. In July 2026 the FDA's Pharmacy Compounding Advisory Committee (PCAC) voted 8-6-1 to recommend adding KPV to the Section 503A bulk drug substances list, although FDA's own reviewers had recommended against it. The vote is advisory; FDA must act through notice-and-comment rulemaking, and no final FDA action has been announced. FDA flagged identity and characterization concerns, including salt forms, for compounds under review. For sport, check the current WADA Prohibited List.
Status changes often. See the regulatory tracker for dated updates.
Quality and identity testing
A good certificate of analysis should confirm identity by mass spectrometry, with the observed mass matching the expected mass shown on this page, and report HPLC purity with the chromatogram. It should specify whether the material is the free acid or the C-terminal amide, since these differ by about 1 Da and may be hard to distinguish without high-resolution MS. Because the peptide is so small, counter-ions make up a large share of the powder, so the salt form and net peptide content are especially important. Very short, polar peptides can retain poorly on standard reverse-phase HPLC, so the method should be appropriate for the analyte.
Open KPV in the sequence analyzer to see the expected [M+H]+ and multiply charged ions for an MS identity check.
For a walkthrough of each section of a certificate, see how to read a COA.
Storage and stability
Store lyophilized KPV sealed at -20 °C, protected from moisture and light, and equilibrate to room temperature before opening; small salt-rich peptides can be hygroscopic. KPV lacks oxidation-prone residues, so it is relatively robust chemically. Prepare solutions in sterile water or buffer for lab use, refrigerate for short-term work, aliquot for frozen storage, and avoid repeated freeze-thaw cycles.
Download the KPV data sheet (PDF): sequence, masses, expected MS ions and handling on one printable page.
Latest research
The newest PubMed-indexed papers that mention KPV in their title or abstract, retrieved through Europe PMC and refreshed automatically. Inclusion is not an endorsement of a paper's findings.
Loading the latest papers…
Frequently asked questions
Is KPV FDA approved?
No. KPV is not approved by the FDA for any use. In July 2026 an FDA advisory committee voted 8-6-1 to recommend adding it to the 503A bulk drug substances list, but the vote is advisory, FDA's reviewers had recommended against, and no final FDA action has been announced.
How is KPV related to alpha-MSH?
KPV is the last three amino acids of alpha-melanocyte-stimulating hormone, a 13-residue peptide. Research interest arose because α-MSH has anti-inflammatory activity in experimental models and early studies suggested that its C-terminal tripeptide retained some of this activity without the sequence linked to pigmentation.
Does KPV cause tanning like melanotan?
KPV lacks the core sequence of α-MSH that is associated with melanocortin-1 receptor activation and pigmentation, and it is not generally described as a pigmenting peptide. Melanotan II is a different, cyclic analogue designed for strong melanocortin receptor activity. Human data on KPV are lacking, so its effects in people are not characterized.
Related compounds
- BPC-157
BPC-157 is a synthetic 15-amino-acid peptide whose sequence was derived from a protein fraction of gastric juice. It is studied mainly in rodent models of gastrointestinal, tendon and soft-tissue injury and is not approved for any use.
- LL-37
LL-37 is the 37-amino-acid antimicrobial peptide released from human cathelicidin hCAP18. It is studied for direct antimicrobial activity and immune-modulating effects in cell, animal and early human studies, and is not approved for any use.
- Melanotan II
Melanotan II is a synthetic cyclic heptapeptide analogue of alpha-melanocyte-stimulating hormone that activates several melanocortin receptors. It is not approved as a medicine anywhere, and regulators have warned about unlicensed tanning products.
- PT-141 (bremelanotide)
PT-141, or bremelanotide, is a cyclic heptapeptide melanocortin receptor agonist derived from melanotan II. It was FDA-approved in 2019 as Vyleesi for hypoactive sexual desire disorder in premenopausal women.
References
- PubMed: all indexed literature on KPV
- ClinicalTrials.gov: registered studies mentioning KPV
Cite this page