KPV — identity, handling and published literature

KPV is the C-terminal tripeptide of α-melanocyte-stimulating hormone, corresponding to residues 11–13 of that hormone, and is supplied as a lyophilised research solid, most commonly as the acetate salt of the free acid H-Lys-Pro-Val-OH.

Presentation and physical properties

α-MSH is a thirteen-residue peptide whose C-terminal three residues are lysine, proline and valine. KPV is that fragment isolated as a discrete molecule. In the parent hormone the C-terminus is amidated; the material catalogued under CAS 67727-97-3 is the free acid, and a C-terminal amide form (H-Lys-Pro-Val-NH₂) also appears in the literature. These are two different molecules and the distinction is frequently left unstated by suppliers and by papers alike.

Reconstitution arithmetic

Reconstitution is a dilution calculation and nothing more. The relationship is that the concentration of the resulting solution equals the mass of solid in the vial divided by the volume of diluent added:

concentration (mg/mL) = vial mass (mg) ÷ diluent volume (mL)

The tables below work that arithmetic for two vial masses commonly encountered in laboratory supply. They state concentration only. Nothing here indicates or implies an amount to be administered to anything.

The molar figures use the free-acid formula mass of 342.43 g/mol, so 10 mg is 29.2 µmol and 50 mg is 146 µmol. If the amide form has in fact been supplied, the formula mass is 341.45 g/mol and every molar figure above is understated by roughly 0.3 per cent — negligible in practice, but it is a different compound and the substitution should be known rather than assumed.

Two arithmetic caveats specific to this molecule are worth stating plainly. First, a labelled mass on a peptide vial is normally the gross mass of the salt, which includes acetate or trifluoroacetate counterions and residual water. Because KPV has two protonatable amines, it can carry two counterion equivalents, and the net peptide content of a vial can therefore sit appreciably below the labelled figure unless a net-peptide assay has been performed and reported. Every concentration derived from label mass alone is an upper bound. Second, small-mass fills are gravimetrically imprecise: a 10 mg fill weighed to ±0.5 mg carries a five per cent uncertainty before any solvent is added, which is larger than the precision the tables above imply.

Storage and stability

In the lyophilised state, kept dry, dark and at −20 °C or below, KPV is a stable solid. Almost all of its practical instability appears once it is in solution, and the routes are unusually easy to enumerate because of what the sequence does not contain.

There is no cysteine, so no disulfide scrambling. No methionine and no tryptophan, so the peptide has essentially no oxidatively labile side chain. No asparagine or glutamine, so no deamidation. No aspartyl-prolyl bond, so no acid-catalysed backbone cleavage at that motif. The degradation chemistry that dominates most peptide stability discussions is therefore largely absent.

What remains is diketopiperazine formation, and it is the dominant route. A tripeptide with proline in the second position is structurally predisposed to intramolecular aminolysis: the pyrrolidine ring constrains the backbone into a conformation in which the N-terminal amine can attack the Pro–Val amide carbonyl, expelling valine and closing a six-membered ring. In a forced-degradation study under acidic, alkaline and hydrogen peroxide stress, Pawar and colleagues reported lys-pro-diketopiperazine as the major degradation product in every case, identified by flow-injection mass spectrometry [22]. That peroxide stress produced the same cyclic degradant rather than an oxidation product is consistent with the absence of an oxidisable residue.

Three practical consequences follow:

• Alkaline conditions are the ones to avoid. Diketopiperazine formation is base-catalysed, because the reaction requires the N-terminal amine in its unprotonated form. Solutions held at or above neutral pH cyclise faster than mildly acidic ones. This is the opposite of the guidance that applies to peptides whose principal liability is acid-catalysed cleavage, and the difference is worth knowing before a buffer is selected.
• Freeze–thaw cycling should be minimised by aliquoting. The mechanical concern with repeated cycling is minor for a molecule this small, but the pH concern is not: in sodium phosphate buffers, disodium hydrogen phosphate crystallises preferentially as ice forms, driving the residual liquid phase substantially alkaline. For a molecule whose main degradation route is base-catalysed, freezing in phosphate is the wrong choice. Water or a non-phosphate buffer avoids the problem.
• Reducing sugars do not belong in the diluent. The free lysine ε-amine will undergo Maillard chemistry with glucose or dextrose. That the amine is reactive enough to matter is established by the published derivatisation work, in which reductive alkylation was carried out at exactly that position [8].

Solutions should be kept refrigerated and used over short periods; no published long-term stability dataset exists at ambient or refrigerated temperature over commercially relevant intervals, so any shelf-life figure quoted for a reconstituted solution is an extrapolation from forced-degradation work rather than a measurement.

Analytical identity

Reversed-phase HPLC

KPV is small, highly polar and cationic, and is consequently weakly retained on octadecylsilane phases. Retention depends on ion pairing rather than on hydrophobic partitioning of the peptide itself. The published stability-indicating method uses a 4.6 × 250 mm, 5 µm C18 column with a gradient of 0.1 per cent trifluoroacetic acid in water against 0.1 per cent trifluoroacetic acid in acetonitrile, and reports separation of the intact peptide from its diketopiperazine degradant and from endogenous skin components, with a limit of detection of 0.01 µg/mL and a limit of quantification of 0.25 µg/mL [22]. A method that elutes KPV close to the void volume has not separated it from anything, and a chromatogram showing a single early peak is not evidence of purity.

Detection wavelength — the point that matters most

None of lysine, proline or valine carries an aromatic ring. KPV therefore has no absorbance maximum at 280 nm and no meaningful absorbance at 254 nm. Detection has to rely on the peptide bond itself, which absorbs in the far UV, so assays are run in the 210–220 nm region. A certificate reporting purity by HPLC at 280 nm has measured essentially nothing for this molecule, and a purity figure obtained at 254 nm is close to meaningless. This is a straightforward way to identify an analytical report that was not generated on the material it claims to describe.

Mass spectrometry

The free acid has the molecular formula C₁₆H₃₀N₄O₄, an average mass of 342.43 and a monoisotopic mass of 342.2267. Electrospray in positive mode gives a singly protonated ion at m/z 343.234 and, because of the two basic amines, a readily observed doubly protonated ion near m/z 172.12.

There is a specific identification trap here. The C-terminal amide form, C₁₆H₃₁N₅O₃, is 0.984 lighter, with a monoisotopic mass of 341.243 and a protonated ion at m/z 342.250. That protonated amide ion sits only about 0.023 from the neutral monoisotopic mass of the free acid. On a low-resolution instrument, or in a report where it is unclear whether a quoted mass is the neutral or the protonated species, the two forms are easily conflated. Resolving them requires either accurate mass to better than about 20 ppm or an explicit statement of which species was measured.

In tandem mass spectrometry, fragmentation is dominated by the proline. Cleavage N-terminal to proline is enhanced relative to other amide bonds, so the y₂ ion corresponding to Pro-Val is a prominent product near m/z 215.1. Low-mass immonium ions provide composition confirmation: proline at 70.065, valine at 72.081 and lysine at 101.107, the last commonly observed together with its ammonia-loss fragment at 84.081.

What area-percent purity does and does not measure

An HPLC purity figure is the area of the main peak expressed as a percentage of total integrated peak area at one wavelength. That is a narrower statement than it appears.

• It is a comparison of UV-absorbing species only. Counterions, residual water, inorganic salts and non-chromophoric organics do not appear. Because KPV is normally an acetate or trifluoroacetate salt, a substantial fraction of the vial contents can be invisible to the assay entirely.
• It says nothing about net peptide content, which is a separate determination — amino acid analysis, nitrogen determination or quantitative NMR. A batch that is 99 per cent pure by area can be well under 90 per cent peptide by mass.
• It says nothing about sequence identity. A single sharp peak of the wrong tripeptide is 100 per cent pure. Only mass spectrometry, and preferably sequencing by tandem MS, addresses identity.
• For this molecule in particular there is a directional bias. The principal degradant, cyclo(Lys-Pro), forms alongside free valine. Free valine has no chromophore beyond its carboxyl group and responds very poorly in the far UV, so a partially degraded sample loses main-peak area to a degradant that is itself under-detected. The measured area percent can therefore overstate purity in a sample degrading by exactly the route this peptide is most prone to.
• Area percent is response-weighted, not mass-weighted. Different species have different molar absorptivity, and at 214 nm response scales roughly with the number of amide bonds, so a dipeptide impurity and a tetrapeptide impurity present at the same molar concentration will not produce the same peak area.

There is no pharmacopoeial monograph for KPV in the British Pharmacopoeia, the European Pharmacopoeia or the United States Pharmacopeia, and no certified reference material. Every purity figure in circulation is therefore against a method the supplier chose, with an impurity specification the supplier set.

What the published literature investigated

What follows describes what published studies did and what they reported. It is a record of the literature, not a statement about what the compound does.

In vitro

The earliest mechanistic work placed KPV alongside its parent hormone in macrophage systems. Mandrika and colleagues examined melanocortin peptides in lipopolysaccharide and interferon-γ-stimulated RAW 264.7 macrophage-like cells, measuring NF-κB DNA binding and nitric oxide production, and reported that the three peptides tested inhibited nitric oxide production with an order of potency of α-MSH ≥ α-MSH(11–13) > α-MSH(1–10); the authors concluded that dual mechanisms were operating, one melanocortin-receptor and cAMP dependent and one not [1].

Cutuli and colleagues tested α-MSH peptides including KPV against Staphylococcus aureus and Candida albicans cultures and reported inhibition of colony formation, with cAMP elevation implicated in the mechanism [2]. Barcellini and colleagues reported reduced HIV-1 expression in chronically infected promonocytic U1 cells exposed to α-MSH and to KPV, and reduced replication in acutely infected monocyte-derived macrophages [3].

Two studies addressed the question of whether a receptor is required at all. Elliott and colleagues examined signalling in HaCaT keratinocytes, normal human keratinocytes and CHO cells transfected with the melanocortin-1 receptor, and reported that α-MSH, KPV and ACTH did not raise cAMP under their conditions but produced rapid intracellular calcium responses [4]. Kelly and colleagues immobilised the closely related tetrapeptide GKPV, that is α-MSH(10–13), on polystyrene beads through polyethylene glycol linkers, so that it could not be internalised, and reported inhibition of TNF-α-stimulated NF-κB activity in an HBL reporter line [5]. That design was chosen specifically to test whether a cell-surface interaction is sufficient.

Land reported on TNF-α- and respiratory syncytial virus-evoked NF-κB signalling in immortalised human bronchial epithelial cells (16HBE14o-) exposed to KPV and to γ-MSH [6]. More recently, Sung and colleagues examined KPV in HaCaT keratinocytes and a three-dimensional reconstructed skin model challenged with particulate matter, reporting effects on reactive oxygen species, caspase-1 activation and interleukin-1β secretion [7].

Separately from the biology, Songok and colleagues published synthetic work modifying the lysine residue of H-KPV-NH₂ by reductive glycoalkylation, which is the clearest published demonstration that the ε-amine is the molecule’s reactive handle [8].

Rodent

Getting and colleagues compared KPV with other α-MSH peptides in a mouse model of crystal-induced peritonitis, and included recessive yellow (e/e) mice carrying a non-functional melanocortin-1 receptor in order to dissect receptor dependence [9].

The largest single body of rodent work concerns chemically induced colitis. Dalmasso and colleagues reported that KPV is a substrate for the di- and tripeptide transporter PepT1 in intestinal epithelial and immune cell lines, and examined the peptide in mouse dextran sodium sulfate and TNBS colitis models [10]. Kannengiesser and colleagues investigated KPV in mouse DSS colitis and in a CD45RB^hi T-cell transfer colitis model, and again used melanocortin-1 receptor null mice to probe mechanism [11]. Viennois and colleagues used transgenic mice overexpressing human PepT1 in intestinal epithelium and PepT1-deleted mice in an azoxymethane/DSS colitis-associated cancer model [12].

From 2010 onwards the majority of published in vivo work is formulation work in which KPV is the payload. Laroui and colleagues reported that mice given DSS followed by KPV-loaded nanoparticles delivered in a polysaccharide hydrogel differed from mice given DSS alone on inflammatory and histological parameters [13]. Xiao and colleagues loaded KPV into hyaluronic acid-functionalised polymeric nanoparticles of approximately 272 nm and reported outcomes in a mouse ulcerative colitis model [14]. Sun and colleagues reported on a cysteamine-grafted γ-polyglutamic acid hydrogel carrying KPV in TNBS-induced colitis in rats [15]; Zhao and colleagues on a KPV-binding double-network hydrogel in the same rat model [16]; and Shao and colleagues on an in situ mucoadhesive hydrogel carrying KPV in a rat model of chemotherapy-induced oral mucositis [17]. Zhang and colleagues co-assembled KPV with rapamycin into carrier-free nanoparticles and reported on vascular calcification in C57BL mice [18].

Outside the gastrointestinal literature, Schaible and colleagues administered α-MSH(11–13) as a single dose in a mouse controlled cortical impact model of traumatic brain injury and reported on inflammatory markers and lesion volume, explicitly framing the tripeptide as an alternative to the parent hormone on grounds of half-life and pigmentary effects [19].

Other in vivo

Bonfiglio and colleagues applied α-MSH(11–13) topically in a rabbit corneal epithelial wound model and reported re-epithelialisation at sixty hours in eight of eight treated corneas, with nitric oxide implicated in the effect; the study also used cultured rabbit corneal epithelial cells [20].

Human

No completed interventional human study of KPV has been published. The nearest human material in the literature is ex vivo: Pawar and colleagues measured permeation of KPV across excised human skin under iontophoresis, microneedle treatment and the two combined, reporting a permeation rate of 4.4 µg/cm²/h with microneedles alone and a thirty-five-fold increase with the combination [21]. Excised skin in a diffusion cell is a transport measurement in human tissue. It is not a clinical trial, it involves no living participant, and it reports nothing about what happens after the molecule crosses the barrier.

Reviews

Narrative reviews covering α-MSH and its C-terminal fragments include Brzoska and colleagues in Endocrine Reviews [23] and in Advances in Experimental Medicine and Biology [24], and Gravina and colleagues on the melanocortin system in inflammatory bowel disease [25]. These summarise the primary literature above; they do not add new data and should not be cited as though they were independent evidence.

Evidence gaps and limitations

This section states what does not exist. It is the most important part of the entry.

There is no completed randomised controlled trial of KPV in humans. There is no published Phase I study. A search of ClinicalTrials.gov returns no registered interventional study with KPV, Lys-Pro-Val or α-MSH(11–13) as the intervention. The entire in vivo evidence base is mouse, rat and rabbit.

There is no published human pharmacokinetic data by any route. Absorption, distribution, metabolism, elimination and half-life in humans are unmeasured. The only human-tissue transport data is a permeation rate across excised skin in a diffusion cell [21], which describes movement through a barrier and nothing beyond it.

There is no published toxicology package. No repeat-dose toxicity study, no genotoxicity battery, no reproductive or developmental toxicity study and no carcinogenicity study appears in the peer-reviewed literature. Statements that KPV is well tolerated rest on the absence of reported adverse findings in short rodent experiments that were not designed or powered to detect them. Absence of reported harm in a fourteen-day colitis experiment is not a safety dataset.

Most in vivo work since 2010 does not test the free peptide. The nanoparticle and hydrogel studies [13]–[18] test a formulation. The peptide is the payload; the vehicle is the variable under development; and the comparator arms are frequently vehicle alone or a differently formulated peptide rather than free KPV at a matched exposure. Several of these papers exist because free KPV performed inadequately on its own, which is the stated rationale for building the carrier. Reading a nanoparticle result as a result about the molecule inverts the point the paper was making.

The mechanism is unresolved and the literature is explicit about that. KPV does not contain the core melanocortin pharmacophore His-Phe-Arg-Trp, and the receptor through which it might act, if any, is not agreed. Mandrika and colleagues proposed dual receptor-dependent and receptor-independent mechanisms [1]; Elliott and colleagues reported no cAMP response in keratinocytes [4]; Getting [9] and Kannengiesser [11] both used melanocortin-1 receptor null animals precisely because the question was open. It remains open.

The rodent colitis models have a poor translational record. Dextran sodium sulfate and TNBS colitis are acute chemical-injury models. They have been the setting for a long list of interventions that did not reproduce in human inflammatory bowel disease. A result in DSS colitis is a result in DSS colitis.

The material tested is often unspecified. Papers do not consistently state whether the free acid or the C-terminal amide was used, and the two are chemically distinct. At least one published study explicitly used H-KPV-NH₂ [8], while the CAS registry entry in common commercial use is the free acid. Where the form is unstated, results cannot be attributed to a specific molecule with confidence.

There is no compendial standard. No British Pharmacopoeia, European Pharmacopoeia or United States Pharmacopeia monograph exists, so there is no agreed assay, no agreed impurity limit and no certified reference material. Batches from different suppliers cannot be compared on a common basis.

There is no long-term stability dataset. The published stability work is forced degradation under stress conditions [22], which identifies degradation routes. It does not establish a shelf life for a reconstituted solution at any temperature.

Regulatory and standards position

United Kingdom. KPV holds no marketing authorisation from the Medicines and Healthcare products Regulatory Agency. No medicinal product containing it is authorised for human or veterinary use. It is not a controlled drug under the Misuse of Drugs Act 1971 or the Misuse of Drugs Regulations 2001, and it is not a psychoactive substance within the meaning of the Psychoactive Substances Act 2016. It is supplied and held as a laboratory chemical. Under MHRA Guidance Note 8 and the doctrine of medicinal product by presentation, a substance becomes a medicinal product in law by virtue of the claims made for it, independent of its own regulatory status — so the way an unauthorised substance is described can itself create a regulatory offence.

European Union. No centrally authorised medicine containing KPV is listed by the European Medicines Agency, and no national marketing authorisation has been identified.

United States. There is no FDA-approved drug product containing KPV, and it is not a listed drug. The FDA operates a separate process under which bulk substances may be nominated and evaluated for pharmacy compounding; movement through that process, in either direction, is administrative and confers no approval, no marketing authorisation and no finding of safety or efficacy. The status of individual peptides within it has changed repeatedly and should be checked against FDA’s own published lists rather than against secondary reporting.

WADA. KPV is not named in any class of the World Anti-Doping Agency Prohibited List. The operative provision is S0, Non-Approved Substances, which captures any pharmacological substance not addressed by another section of the List and with no current approval by any governmental regulatory health authority for human therapeutic use. Substances captured by S0 are prohibited at all times, in and out of competition. This is a class capture rather than a named listing, and the classification would change if the molecule were ever authorised somewhere.

Standards. No pharmacopoeial monograph and no certified reference material exists in any jurisdiction.

Laboratory handling and safety

There is no published toxicology package for KPV, so no occupational exposure limit has been derived and none can be. The correct posture towards a substance with no toxicological characterisation is to minimise exposure by default rather than to reason from an absence of reported harm.

• Personal protective equipment. Nitrile gloves, safety spectacles and a laboratory coat as a minimum. Weighing and handling of the dry lyophilised solid should be done in a ventilated enclosure, a powder-weighing hood or a balance safety enclosure: lyophilised cakes are light, electrostatic and readily become airborne, and inhalation is the exposure route hardest to control and easiest to overlook.
• Reconstitution. Add diluent down the vial wall rather than directly onto the cake, and allow the solid to dissolve without vigorous agitation. Shaking generates aerosol on opening and creates an air-liquid interface at which peptides adsorb and denature. Vent pressure carefully; a vial stoppered under vacuum will draw diluent in abruptly.
• Spills. Dry powder should not be swept or brushed, which re-aerosolises it. Dampen with a lightly wetted absorbent pad, wipe inwards from the edge, and place waste in a sealed bag. Liquid spills should be absorbed, the area wiped with detergent solution and then with water. Change gloves after clean-up.
• Disposal. Dispose of the peptide, contaminated consumables and unused solutions as laboratory chemical waste through a licensed contractor and in accordance with the Hazardous Waste (England and Wales) Regulations 2005 or the equivalent devolved provisions. Sharps into a UN-approved sharps container. Nothing goes to drain and nothing goes into general refuse.
• Record-keeping. Record the supplier, batch or lot number, quantity received, date received and storage location on receipt. On reconstitution, record the date, the diluent and its lot, the volume added and the calculated concentration, and label the vial with that information plus the operator’s initials. Retain the certificate of analysis and, where possible, the underlying chromatogram and mass spectrum rather than only the summary figures — a summary certificate cannot be re-examined and a chromatogram can. Where the supplier does not state whether the material is the free acid or the C-terminal amide, record that the form is unstated rather than assuming one.
• Freeze–thaw. Aliquot on first reconstitution into single-use volumes. This is a stability measure as well as a contamination measure; see Analytical identity and the storage section above for why phosphate buffers in particular are a poor choice for frozen storage of this molecule.
• COSHH. A COSHH assessment is required before first use. It should record explicitly that no toxicological data exists, since that absence is itself the finding that drives the control measures.

References

1. Mandrika I, Muceniece R, Wikberg JE. Effects of melanocortin peptides on lipopolysaccharide/interferon-gamma-induced NF-kappaB DNA binding and nitric oxide production in macrophage-like RAW 264.7 cells: evidence for dual mechanisms of action. Biochem Pharmacol. 2001;61(5):613–21. Model: in vitro, RAW 264.7 murine macrophage-like cells. PMID 11239505
2. Cutuli M, Cristiani S, Lipton JM, Catania A. Antimicrobial effects of alpha-MSH peptides. J Leukoc Biol. 2000;67(2):233–9. Model: in vitro, Staphylococcus aureus and Candida albicans cultures, human neutrophils. PMID 10670585
3. Barcellini W, Colombo G, La Maestra L, et al. Alpha-melanocyte-stimulating hormone peptides inhibit HIV-1 expression in chronically infected promonocytic U1 cells and in acutely infected monocytes. J Leukoc Biol. 2000;68(5):693–9. Model: in vitro, U1 promonocytic cells and monocyte-derived macrophages. PMID 11073109
4. Elliott RJ, Szabo M, Wagner MJ, et al. alpha-Melanocyte-stimulating hormone, MSH 11-13 KPV and adrenocorticotropic hormone signalling in human keratinocyte cells. J Invest Dermatol. 2004;122(4):1010–9. Model: in vitro, HaCaT keratinocytes, normal human keratinocytes, CHO cells transfected with MC-1R. PMID 15102092
5. Kelly JM, Moir AJ, Carlson K, et al. Immobilized alpha-melanocyte stimulating hormone 10-13 (GKPV) inhibits tumor necrosis factor-alpha stimulated NF-kappaB activity. Peptides. 2006;27(2):431–7. Model: in vitro, HBL cells with NF-kappaB-luciferase reporter; peptide immobilised on polystyrene beads. PMID 16274845
6. Land SC. 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. Int J Physiol Pathophysiol Pharmacol. 2012;4(2):59–73. Model: in vitro, immortalised human bronchial epithelial cells (16HBE14o-). PMID 22837805
7. Sung J, Ju SY, Park S, et al. Lysine-Proline-Valine peptide mitigates fine dust-induced keratinocyte apoptosis and inflammation by regulating oxidative stress and modulating the MAPK/NF-kappaB pathway. Tissue Cell. 2025;95:102837. Model: in vitro, HaCaT keratinocytes and a three-dimensional reconstructed skin model. PMID 40073467
8. Songok AC, Panta P, Doerrler WT, et al. Structural modification of the tripeptide KPV by reductive “glycoalkylation” of the lysine residue. PLoS One. 2018;13(6):e0199686. Model: in vitro, synthetic chemistry and antimicrobial assay. PMID 29953505
9. Getting SJ, Schiöth HB, Perretti M. Dissection of the anti-inflammatory effect of the core and C-terminal (KPV) alpha-melanocyte-stimulating hormone peptides. J Pharmacol Exp Ther. 2003;306(2):631–7. Model: rodent, mouse crystal-induced peritonitis, including MC1-R null (recessive yellow e/e) mice. PMID 12750433
10. Dalmasso G, Charrier-Hisamuddin L, Nguyen HT, et al. PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation. Gastroenterology. 2008;134(1):166–78. Model: rodent, mouse DSS and TNBS colitis, with Caco2-BBE, HT29-Cl.19A and Jurkat cell work. PMID 18061177
11. Kannengiesser K, Maaser C, Heidemann J, et al. Melanocortin-derived tripeptide KPV has anti-inflammatory potential in murine models of inflammatory bowel disease. Inflamm Bowel Dis. 2008;14(3):324–31. Model: rodent, mouse DSS colitis and CD45RB(hi) transfer colitis, including MC1R-null mice. PMID 18092346
12. Viennois E, Ingersoll SA, Ayyadurai S, et al. Critical role of PepT1 in promoting colitis-associated cancer and therapeutic benefits of the anti-inflammatory PepT1-mediated tripeptide KPV in a murine model. Cell Mol Gastroenterol Hepatol. 2016;2(3):340–357. Model: rodent, hPepT1-transgenic and PepT1-knockout mice, AOM/DSS colitis-associated cancer. PMID 27458604
13. Laroui H, Dalmasso G, Nguyen HT, et al. Drug-loaded nanoparticles targeted to the colon with polysaccharide hydrogel reduce colitis in a mouse model. Gastroenterology. 2010;138(3):843–53.e1–2. Model: rodent, mouse DSS colitis, KPV-loaded nanoparticles. PMID 19909746
14. Xiao B, Xu Z, Viennois E, et al. Orally Targeted Delivery of Tripeptide KPV via Hyaluronic Acid-Functionalized Nanoparticles Efficiently Alleviates Ulcerative Colitis. Mol Ther. 2017;25(7):1628–1640. Model: rodent, mouse ulcerative colitis, with colonic epithelial cell and macrophage work in vitro. PMID 28143741
15. Sun J, Xue P, Liu J, et al. Self-Cross-Linked Hydrogel of Cysteamine-Grafted γ-Polyglutamic Acid Stabilized Tripeptide KPV for Alleviating TNBS-Induced Ulcerative Colitis in Rats. ACS Biomater Sci Eng. 2021;7(10):4859–4869. Model: rodent, rat TNBS colitis. PMID 34547895
16. Zhao Y, Xue P, Lin G, et al. A KPV-binding double-network hydrogel restores gut mucosal barrier in an inflamed colon. Acta Biomater. 2022;143:233–252. Model: rodent, rat TNBS colitis. PMID 35245681
17. Shao W, Chen R, Lin G, et al. In situ mucoadhesive hydrogel capturing tripeptide KPV: the anti-inflammatory, antibacterial and repairing effect on chemotherapy-induced oral mucositis. Biomater Sci. 2021;10(1):227–242. Model: rodent, rat chemotherapy-induced oral mucositis. PMID 34846053
18. Zhang L, Li D, Aierken Y, et al. KPV and RAPA Self-Assembled into Carrier-Free Nanodrugs for Vascular Calcification Therapy. Adv Healthc Mater. 2024;13(32):e2402320. Model: rodent, C57BL mice, vascular calcification. PMID 39252648
19. Schaible EV, Steinsträßer A, Jahn-Eimermacher A, et al. Single administration of tripeptide α-MSH(11-13) attenuates brain damage by reduced inflammation and apoptosis after experimental traumatic brain injury in mice. PLoS One. 2013;8(8):e71056. Model: rodent, mouse controlled cortical impact. PMID 23940690
20. Bonfiglio V, Camillieri G, Avitabile T, et al. Effects of the COOH-terminal tripeptide alpha-MSH(11-13) on corneal epithelial wound healing: role of nitric oxide. Exp Eye Res. 2006;83(6):1366–72. Model: rabbit, in vivo corneal epithelial wound and cultured rabbit corneal epithelial cells. PMID 16965771
21. Pawar K, Kolli CS, Rangari VK, Babu RJ. Transdermal Iontophoretic Delivery of Lysine-Proline-Valine (KPV) Peptide Across Microporated Human Skin. J Pharm Sci. 2017;106(7):1814–1820. Model: ex vivo human skin in diffusion cells; not a clinical study. PMID 28343991
22. Pawar KR, Mulabagal V, Smith F, et al. Stability-indicating HPLC assay for lysine-proline-valine (KPV) in aqueous solutions and skin homogenates. Biomed Chromatogr. 2015;29(5):716–21. Model: analytical method development and forced degradation. PMID 25298219
23. Brzoska T, Luger TA, Maaser C, et al. Alpha-melanocyte-stimulating hormone and related tripeptides: biochemistry, antiinflammatory and protective effects in vitro and in vivo, and future perspectives for the treatment of immune-mediated inflammatory diseases. Endocr Rev. 2008;29(5):581–602. Model: review. PMID 18612139
24. Brzoska T, Böhm M, Lügering A, et al. Terminal signal: anti-inflammatory effects of α-melanocyte-stimulating hormone related peptides beyond the pharmacophore. Adv Exp Med Biol. 2010;681:107–16. Model: review. PMID 21222263
25. Gravina AG, Pellegrino R, Durante T, et al. The Melanocortin System in Inflammatory Bowel Diseases: Insights into Its Mechanisms and Therapeutic Potentials. Cells. 2023;12(14):1889. Model: review. PMID 37508552

Research use only

KPV is a laboratory research chemical, supplied and held for research use only. It is not a medicine. It is not authorised by the MHRA, the EMA or the FDA for human or veterinary use, and it is not approved for administration to humans or to animals, for use as a food or food ingredient, for use in cosmetics, or for any household purpose. Nothing in this entry is a recommendation to administer it to anything.

This entry is a record of published literature and of physicochemical and handling data. Reporting what a study investigated and what it reported is a statement about that study. It is not a statement that the compound produces any effect, and it must not be read as one. No claim is made or implied here that KPV treats, prevents, cures, mitigates or affects any disease or condition in any species.

NovoVita does not supply KPV as a single-compound presentation. It is included here because this reference library covers the compound field rather than the product catalogue. KPV appears as one component of the KLOW blend.