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Free U.S. shipping on orders over $150KPV is a short bioactive peptide composed of three amino acids: lysine (K), proline (P), and valine (V) [1]. It is derived from the larger parent molecule α-melanocyte-stimulating hormone (α-MSH), a peptide hormone that modulates inflammation, pigmentation, circadian rhythm, and immune responses [1].
Unlike the full α-MSH sequence, KPV represents the minimal active fragment capable of exerting anti-inflammatory and protective effects in experimental settings.
Because of its small size, KPV is more stable and potentially more amenable to topical or localized delivery compared to its larger parent peptide [2].
KPV is a promising subject of investigation in areas where inflammation and tissue degeneration play central roles, including aging-related disorders.
KPV is thought to act through interactions with the melanocortin 1 receptor (MC1R), a G-protein-coupled receptor expressed in a variety of tissues, including skin, intestinal epithelial cells, and immune cells [3].
One of the most consistent findings across KPV research is its anti-inflammatory activity, particularly in epithelial tissues such as the gut and skin.
In preclinical studies, KPV downregulates pro-inflammatory cytokines, including:
At the same time, KPV enhanced anti-inflammatory mediators, helping to restore immune balance in tissues that were chronically stressed or damaged.
Wound healing is a complex process that requires coordinated activity between keratinocytes, fibroblasts, immune cells, and vascular networks [7]. With aging, this regenerative capacity declines, delaying healing and increasing the risk of chronic wounds and scarring.
Research on KPV suggests that it may play a role in supporting tissue repair by modulating inflammation and stimulating cellular regeneration [8].
Animal studies indicate that KPV significantly accelerates keratinocyte migration and proliferation, which promote the re-epithelialization of damaged skin and cornea [9]. By dampening the inflammatory cascade, KPV creates a more favorable environment for tissue recovery [1].
In parallel, KPV has been shown to influence fibroblast activity and extracellular matrix remodeling, processes that underpin scar formation, collagen deposition, and the restoration of skin integrity [10].
In mouse models, KPV accelerates full-thickness wound closure and reduces scarring compared to untreated controls [11]. KPV accomplishes this through increased angiogenesis and collagen deposition.
The peptide appears to limit oxidative and inflammatory injury and enhance reparative signaling, striking a balance between protecting cells from further damage and promoting regeneration.
In the gut, inflammation disrupts epithelial barrier integrity, leading to increased permeability and impaired nutrient absorption [12]. KPV may counteract this by supporting epithelial repair and reducing inflammatory signaling via inhibiting NF-𝛋B and MAPK signaling pathways [4].
In murine models of inflammatory bowel disease, KPV led to significantly earlier recovery and stronger regain of body weight. The peptide preserved epithelial integrity, reduced oxidative injury, and supported mucosal repair [13].
In dermatological research, KPV has demonstrated the ability to:
In animal models of dermatitis and wound healing, KPV has demonstrated the ability to reduce redness, irritation, and swelling [14]. By balancing cytokine activity and oxidative stress, KPV may treat inflammatory skin conditions and restore healthy skin.
KPV may also be particularly relevant to skin aging, where low-level chronic inflammation accelerates collagen degradation, barrier dysfunction, and visible changes [15].
These effects are consistent with its origin as a fragment of α-MSH, a peptide historically studied for its skin-protective properties.
KPV is generally well tolerated in experimental settings [16]. Unlike full-length α-MSH or other melanocortin peptides, KPV does not significantly influence pigmentation, reducing the risk of unwanted skin-darkening effects.
Preclinical studies report no major systemic toxicity or adverse events, and topical or localized administration appears safe. Although extremely rare, applications of proteins or peptides may run the risk of local irritation or allergic reactions [17].
The evidence base remains limited, with most data derived from animal models, in vitro experiments, or small pilot human studies. Long-term safety, optimal dosing, and potential interactions of KPV with other compounds have yet to be fully established.
Research Use Only. All findings described above are derived from preclinical studies (animal models and in vitro experiments). KPV is not approved by the FDA for any diagnostic or therapeutic use in humans. Genesis Peptides makes no claims regarding human clinical efficacy. This product is sold exclusively for laboratory research.
Every lot undergoes six independent assays before release. Results are published in the lot-specific Certificate of Analysis.
KPV, also called alpha-MSH(11-13), is a COOH-terminal tripeptide that carries the effective message sequence of alpha-MSH. KPV is the tripeptide Lys-Pro-Val, which is derived from alpha-MSH (alpha-melanocyte-stimulating hormone). In a mouse model of colitis, KPV delivered by engineered nanoparticles to the colon was assessed for therapeutic efficacy.
KPV, the Lys-Pro-Val sequence, is the C-terminal sequence of alpha-MSH, which is an endogenous linear tridecapeptide. This sequence is written as alpha-MSH(11-13), so it corresponds to residues 11 to 13 of alpha-MSH. Lys-Pro-Val lies within the alpha-MSH(6-13) sequence, which also contains the invariant melanocortin core His-Phe-Arg-Trp (6-9). The sequence alpha-MSH(11-13) is described as important for antimicrobial activity.
The C-terminal tripeptide Lys-Pro-Val (KPV) of alpha-MSH is the sequence to which alpha-MSH's anti-inflammatory and antimicrobial activities have been traced. The sequence alpha-MSH(11-13), which is Lys-Pro-Val, is described as important for antimicrobial activity. The authors describe a novel X-Pro-D/L-Val peptide type, similar to the short melanocortin peptides, that has antibacterial activity, and Ac-Lys-Pro-Val-NH2 is one peptide of this type.
In CD45RB(hi) transfer colitis in mice, KPV treatment led to recovery, regain of body weight, and reduced inflammatory changes on histology. In mice, oral administration of KPV reduced the incidence of DSS- and TNBS-induced colitis, indicated by a decrease in pro-inflammatory cytokine expression. In dextran sodium sulfate-treated mice, KPV-loaded nanoparticles protected against inflammatory and histologic parameters compared with DSS alone. Across two murine models of colitis, KPV showed significant anti-inflammatory effects, which appear to be at least partially independent of MC1R signaling.
In tests on human astrocytes in vitro, alpha-MSH (11-13), another name for KPV, reduced TNF-alpha. The same tests found that alpha-MSH (1-13) also reduced TNF-alpha in these human astrocytes. This effect was observed in cultured cells, not in people.
In rabbits, eight out of eight corneas treated with KPV or SP were completely re-epithelized sixty hours after treatment. None of the placebo-treated corneas were re-epithelized in that study. The authors concluded that KPV may facilitate corneal epithelial wound healing in rabbits, with a mechanism that may involve nitric oxide disposition in corneal tissue.
In a rabbit study, pre-treatment with the nitric oxide synthase inhibitor L-NAME inhibited the facilitating effect of KPV on corneal epithelial wound healing. The authors concluded that KPV may facilitate corneal epithelial wound healing in rabbits through a mechanism that may involve nitric oxide disposition in corneal tissue.
In in vitro experiments, uptake studies used cold KPV as a competitor for a PepT1 radiolabelled substrate and used [(3)H]KPV to determine the kinetic characteristics of KPV uptake. In animal studies, KPV (Lys-Pro-Val), a tripeptide transported by PepT1, was able to prevent carcinogenesis in wild-type mice. In animal studies, when KPV was administered to PepT1-knockout mice, it did not produce the inhibitory effect on tumorigenesis seen in wild-type mice.
In an in vitro study of cultured cells, KPV inhibited activation of NF-kappaB, a pathway that is known to enhance viral expression. The same study indicated that the peptide's influence on viral replication is at the transcriptional level.
In vitro, KPV held in an SH-PGA hydrogel showed enhanced stability, as it retained its anti-inflammatory activity and its ability to promote cell migration after 2 hours at 37 °C. In vitro, a PMSP hydrogel provided KPV with better stability when KPV was exposed to a high temperature of 50 °C.
In in vitro studies, a fluorescent probe named DCM-KPV was made by conjugating KPV to the DCM chromophore. The study reports that the KPV moiety of this probe gives a specific receptor-targeted interaction with PepT1. Separately, in in vitro uptake experiments, KPV was studied as a PepT1 competitor and as [(3)H]KPV to determine the kinetic characteristics of its uptake.
FOR RESEARCH USE ONLY — Products are sold exclusively for in vitro and preclinical laboratory research. Not for human consumption or administration. Not intended for diagnostic or therapeutic use. These statements have not been evaluated by the FDA.