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Molecular Weight
Purity
Storage
Appearance
Solubility
01
KPV is the tripeptide Lys-Pro-Val, which corresponds to residues 11–13 at the C-terminal end of α-melanocyte-stimulating hormone (α-MSH). It is one of the smallest peptides in this catalogue.
It has been studied as a minimal fragment of α-MSH in cell-based models of inflammatory signalling, and it is a demanding test case for analytical methods because of its small size, early HPLC elution and weak UV absorbance. It is supplied as a lyophilized reference material for in vitro research only, and no biological function is claimed for it here.
02
Each of KPV’s three residues contributes distinct properties.
Lys1
Carries both the N-terminal amine and a side-chain amine, so the peptide has a net positive charge of about +1 at neutral pH and is very water-soluble.
Pro2
The proline ring restricts backbone flexibility. Its position directly after the N-terminal residue also makes the molecule a substrate for X-Pro-cleaving enzymes and prone to cyclisation (see Stability & Handling).
Val3
A branched aliphatic residue at the C-terminus, giving the peptide its only modest hydrophobic character. The C-terminus is a free acid.
Small size
Three residues are too few to form helices or sheets, and there are no aromatic residues, so UV absorbance comes only from the two peptide bonds.
03
KPV has been studied in vitro as a minimal fragment of α-MSH.
Melanocortin context
The C-terminal Lys-Pro-Val segment of α-MSH has been examined for whether it retains any receptor-related activity of the parent hormone. As a three-residue fragment, it lacks the core His-Phe-Arg-Trp sequence that drives high-affinity melanocortin receptor binding.
Inflammatory signalling
Cell-culture studies have examined effects on NF-κB pathway activation and inflammatory cytokine expression, as well as uptake through peptide transporters such as PepT1 in intestinal epithelial cell models.
Structure–activity studies
Used to explore how much of a signalling effect can be retained by very short peptide sequences.
All observations described here come from controlled in vitro systems and do not establish function in living organisms.
04
Small-peptide HPLC
A challenging test compound for methods that must retain and detect very polar, early-eluting peptides with weak UV absorbance.
LC-MS method development
Its single charge state and simple fragmentation make it a clean model for small-peptide MS methods.
Peptidase studies
A model substrate for X-Pro-cleaving enzymes such as DPP-IV, and for studying diketopiperazine formation.
Blend analysis
A component of some multi-peptide research blends, where detecting a 342 Da tripeptide alongside much larger peptides is a methodological challenge.
05
Storage
Store the lyophilized powder at −20 °C, sealed and desiccated. Let the vial reach room temperature before opening.
Diketopiperazine formation
Peptides with proline in the second position can cyclise, forming cyclo(Lys-Pro) and releasing valine. This is favoured in solution at neutral to basic pH and higher temperatures, so solutions should be used promptly.
Enzymatic cleavage
The Lys-Pro N-terminus is recognised by dipeptidyl peptidase-IV, which removes Lys-Pro. Account for this in cell or serum-containing media.
Reconstitution
Dissolves readily in water or aqueous buffer. Prepare fresh, or aliquot and freeze; avoid repeated freeze–thaw cycles.
Labware
Use low-binding polypropylene tubes; small peptides can be lost to glass and polystyrene surfaces.
06
KPV’s small size and polarity call for adjusted methods.
HPLC
KPV elutes early on reversed-phase columns. A low starting organic content with a shallow initial gradient, a polar-embedded or aqueous-compatible C18 column, or HILIC helps separate it from the void volume. Detect at about 205–210 nm for better sensitivity.
Mass spectrometry
Positive-mode ESI gives [M+H]⁺ at m/z 343.2 (monoisotopic) and often a sodium adduct at m/z 365.2. MS/MS shows b₂ at m/z 226.2, y₂ at 215.1, y₁ at 118.1 and lysine immonium ions at 101.1 and 84.1.
Quantification in complex samples
In biological or blend samples, LC-MS/MS is preferred over UV, ideally with a stable-isotope-labelled KPV internal standard.
Impurity profile
Typical checks include cyclo(Lys-Pro), free valine, dipeptides from incomplete synthesis (Lys-Pro, Pro-Val) and counter-ion content.
07
It is the C-terminal tripeptide (residues 11–13) of α-melanocyte-stimulating hormone, a 13-residue peptide derived from pro-opiomelanocortin.
It is very small and polar, so it elutes early on reversed-phase columns, and it has no aromatic residues, so UV absorbance is weak. Detection at 205–210 nm, adjusted gradients or HILIC, and LC-MS are typically needed.
It restricts backbone flexibility. Because it sits in position 2, it also makes KPV a substrate for DPP-IV, which cleaves after X-Pro, and allows cyclisation to cyclo(Lys-Pro), a diketopiperazine. It does not protect KPV from these N-terminal processes.
KPV appears in some multi-peptide blends alongside BPC-157, TB-500 and GHK-Cu. Check the blend listings in this catalogue for the exact composition of each product.
A stable-isotope-labelled version of KPV (for example with ¹³C/¹⁵N-labelled lysine or valine) used with LC-MS/MS. It behaves almost identically to KPV but is distinguished by mass, correcting for matrix effects and recovery.
Cyclisation of the N-terminal Lys-Pro into a diketopiperazine, which releases valine. It is favoured in solution at neutral to basic pH and higher temperatures. In biological media, cleavage by DPP-IV is also important.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
KPV Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/structural-research-peptides/kpv/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
