KPV 10 mg

KPV is a tripeptide. Its three residues are lysine, proline and valine, written K-P-V in one-letter code and Lys-Pro-Val in three-letter code. The registered material is the free acid, H-Lys-Pro-Val-OH, with molecular formula C16H30N4O4 and a molecular weight of 342.43 g/mol under CAS number 67727-97-3. Catalogues also list it as alpha-MSH (11-13) and as ACTH (11-13), which are names for the same sequence rather than different compounds. At 342 daltons it is one of the smallest molecules sold in this category, roughly a fourteenth the mass of a peptide such as retatrutide.

The sequence is the carboxy-terminal end of alpha-melanocyte-stimulating hormone. Alpha-MSH is a thirteen-residue peptide, SYSMEHFRWGKPV, printed in that form by Cutuli and colleagues in 2000. It is cleaved from the precursor protein pro-opiomelanocortin, and in its native state it carries an acetyl group at the amino terminus and an amide at the carboxy terminus. KPV corresponds to positions 11, 12 and 13 of that chain. One chemical detail is worth stating precisely: because the parent hormone ends in a valinamide, the free-acid KPV registered under 67727-97-3 is not chemically identical to the terminal three residues as they exist inside alpha-MSH. PubChem indexes the compound under the explicit synonym "alpha-MSH (11-13) (free acid)" for this reason.

The residues themselves account for most of its chemistry. Lysine contributes a basic, positively charged side chain at physiological pH. Proline is a cyclic imino acid whose pyrrolidine ring locks the backbone into a restricted set of conformations, so the molecule is conformationally stiffer than a three-residue chain would otherwise be. Valine adds a branched aliphatic side chain. The material is produced by solid-phase peptide synthesis, purified by reversed-phase HPLC, and supplied lyophilised. Some suppliers list an acetate salt rather than the free acid while still quoting CAS 67727-97-3, which changes both the correct formula and the correct mass, so a certificate of analysis should be read against the specific material tested.

The most cited work on this specific tripeptide concerns how it enters cells. Dalmasso et al. (2008, Gastroenterology) tested KPV in human intestinal epithelial lines Caco2-BBE and HT29-Cl.19A and in Jurkat T cells, and reported that nanomolar concentrations inhibited activation of NF-kappaB and MAP kinase signalling and reduced pro-inflammatory cytokine secretion. Using tritiated KPV and competition against a radiolabelled PepT1 substrate, the authors characterised uptake kinetics and concluded that entry was mediated by PepT1, a di- and tripeptide transporter normally expressed in small intestine and induced in colon during inflammatory bowel disease. In the same paper, KPV added to the drinking water of mice reduced the incidence of DSS- and TNBS-induced colitis, assessed histologically and by pro-inflammatory cytokine mRNA expression.

Two independent groups have examined whether the effect requires a melanocortin receptor, and both reported that it does not, at least not fully. Kannengiesser et al. (2008, Inflammatory Bowel Diseases) ran DSS colitis and CD45RB-high transfer colitis in mice, recording body weight, colonic histology and myeloperoxidase activity, and additionally treated MC1Re/e animals carrying a non-functional melanocortin-1 receptor. Effects persisted in those animals, and the authors concluded the activity was at least partially independent of MC1R signalling. Earlier, Getting et al. (2003, Journal of Pharmacology and Experimental Therapeutics) used a crystal-induced peritonitis model in mice and reported that the reduction in polymorphonuclear leukocyte accumulation seen with KPV was not blocked by the MC3/MC4 receptor antagonist SHU9119. In the same paper, macrophage activation measured as release of KC and interleukin-1beta was inhibited by alpha-MSH and by the MC3/4 agonist MTII but not by KPV, and KPV failed to increase cAMP. The authors concluded that KPV is unlikely to mediate its effects through melanocortin receptors and is more likely to act through inhibition of interleukin-1beta functions.

Work outside the gut is thinner but not absent. Land (2012, International Journal of Physiology, Pathophysiology and Pharmacology) measured TNF-alpha- and respiratory syncytial virus-evoked NF-kappaB signalling in an immortalised human bronchial epithelial line (16HBE14o-) and reported dose-dependent inhibition of NF-kappaB, matrix metalloproteinase-9 activity, and IL-8 and eotaxin secretion. The paper associates the KPV effect with its nuclear import, IkappaB-alpha stabilisation and suppressed nuclear translocation of tagged p65RelA. In the same study gamma-MSH produced a comparable anti-inflammatory outcome but, in contrast to KPV, required MC3R, which is consistent with the receptor-independence reported by the peritonitis and colitis groups. In skin cells, Elliott et al. (2004, Journal of Investigative Dermatology) reported a negative result that is often overlooked: no elevation of cyclic AMP was detected in either HaCaT or normal human keratinocytes on exposure to alpha-MSH, KPV or ACTH peptides, although rapid intracellular calcium responses were observed, and in Chinese hamster ovary cells stably transfected with the MC1 receptor both alpha-MSH and the KPV peptides elevated intracellular calcium.

Two further lines of investigation are narrower. Cutuli et al. (2000, Journal of Leukocyte Biology) tested alpha-MSH and its C-terminal tripeptide against Staphylococcus aureus and Candida albicans, reporting inhibition of S. aureus colony formation and reduced viability and germ tube formation in C. albicans, with the authors proposing that the effect could be mediated by an increase in cellular cAMP. More recently Sung et al. (2025, Tissue and Cell) exposed HaCaT keratinocytes to PM10 particulate matter and reported that treatment with 50 micrograms per millilitre of KPV restored cell viability and reduced interleukin-1beta, with measured effects on reactive oxygen species production, ERK and p38 MAP kinase, NF-kappaB and caspase-1 activation, extended to a three-dimensional skin model.

The overall state of the record should be read carefully. Every study cited above is in vitro or in rodents. A search of the ClinicalTrials.gov v2 API in July 2026 for KPV and for lysyl-prolyl-valine returned no registered studies, and a broader Lys-Pro-Val query returned only unrelated trials matched on stray tokens rather than any study of the tripeptide. There is therefore no human trial data, no established human pharmacokinetics and no human safety record. The rodent work also used delivery routes that do not transfer directly between studies: drinking water in one colitis model, systemic injection in others, and topical or formulated systems in the dermatological work. Molecules of this size clear quickly as a general matter, and much of the subsequent literature is formulation chemistry aimed at that problem rather than new pharmacology.