KPV

KPV (Lys-Pro-Val) is the C-terminal tripeptide of α-melanocyte-stimulating hormone (α-MSH, residues 11–13). At three residues, it is one of the smallest peptides documented to retain the parent hormone’s anti-inflammatory activity, making it a frequent reference compound in structure-activity studies of small anti-inflammatory peptides.

Published mechanism studies establish that KPV’s effects operate largely independently of melanocortin receptors. The dominant pathway is direct intracellular NF-κB inhibition: the tripeptide enters cells via passive diffusion or peptide-transporter-mediated uptake (PepT1 / SLC15A1), where it prevents p65-IκBα dissociation and blocks the transcription of pro-inflammatory cytokines (TNF-α, IL-1β, IL-6, IL-8) at the source.

Recent 2026 work (Lee et al., Cytotechnology, PMID 42064835) extended KPV’s mechanism profile from classical anti-inflammation into hepatic lipid metabolism, demonstrating ROS-dependent regulation of the PPARγ pathway in HepG2 cells. Active translational delivery research is developing targeted KPV systems for inflammatory bowel disease — hydrogel microsphere (Jeong et al., 2025, PMID 40030207) and temperature-sensitive hydrogel (Li et al., 2024, PMID 38289234) approaches.

Every Artemis Labs lot ships with a third-party Certificate of Analysis confirming identity (MS), purity (≥99% by reverse-phase HPLC), and endotoxin testing (≤0.5 EU/mg, LAL assay). Supplied as lyophilized white powder, 10 mg/vial, for in-vitro receptor, cell-culture, and pre-clinical research applications.

For research use only. Not for human or veterinary use.

Science & Research

MECHANISM OF ACTION

KPV (Lys-Pro-Val) corresponds to residues 11–13 of alpha-melanocyte-stimulating hormone (α-MSH) — the C-terminal tripeptide of the parent hormone. The published mechanism is a melanocortin-receptor-independent anti-inflammatory pathway:

1. Cellular Uptake — KPV is small enough (three residues) to enter cells via passive diffusion or peptide-transporter-mediated uptake. Peptide Transporter 1 (PepT1 / SLC15A1) — the same gateway that absorbs dietary di- and tripeptides — has been characterized as one recognized uptake mechanism.

2. NF-κB Pathway Inhibition — Once intracellular, KPV directly suppresses nuclear factor-kappa B (NF-κB) activation. NF-κB is the master transcriptional switch for pro-inflammatory cytokines: TNF-α, IL-1β, IL-6, IL-8. KPV blocks p65-IκBα complex dissociation and prevents p65 nuclear translocation, suppressing inflammation at the transcriptional level rather than the receptor level.

3. Selective Localization — Because NF-κB is preferentially activated in inflamed tissue, KPV’s effects concentrate at sites of dysregulation while leaving non-inflamed tissue largely unaffected in published research models. This selectivity distinguishes KPV from broadly immunosuppressive interventions.

2024–2026 MECHANISM RESEARCH

– Hepatic lipid metabolism / PPARγ pathway (Lee et al., 2026, PMID 42064835): Lys-Pro-Val attenuated hepatic lipid accumulation in HepG2 cells via ROS-dependent regulation of the PPARγ pathway. This is the single most directly KPV-relevant new finding in the 2024–2026 window, extending the mechanism profile from anti-inflammation into hepatic lipid metabolism research.

– Hydrogel microsphere delivery for IBD research (Jeong et al., 2025, PMID 40030207): Multicompartmental hydrogel microspheres with a concentric thin oil layer were engineered to protect KPV during transit and deliver it to colonic epithelium while preserving anti-inflammatory activity.

– Temperature-sensitive hydrogel (Li et al., 2024, PMID 38289234): Growth-factor-loaded temperature-sensitive hydrogel acting as a biomimetic mucus layer attenuated ulcerative colitis in murine models by repairing mucosal barriers; KPV positioned within the IBD therapeutic-agent context.

– 2026 reviews (Renke 2026, PMID 42123471; Mendias 2026, PMID 41966639; Mavrych 2026, PMID 42021992): KPV continues to be reviewed as a viable anti-inflammatory peptide within broader peptide-therapy literature.

STRUCTURE-ACTIVITY CONTEXT

KPV’s mechanism is intentionally minimalist — three residues, no melanocortin-receptor binding required, no copper coordination chemistry — which is why it is widely used as a reference compound in structure-activity studies of small anti-inflammatory peptides.

ANALYTICAL SPECIFICATIONS

– Sequence: Lys-Pro-Val (α-MSH residues 11–13)
– Molecular Formula: C₁₆H₃₀N₄O₄
– Molecular Weight: ~342.4 g/mol
– Parent peptide: α-melanocyte-stimulating hormone (13 residues)
– Purity Standard: ≥99% by reverse-phase HPLC
– Storage (lyophilized): –20 °C, desiccated, protected from light
– Form: Lyophilized white powder, 10 mg/vial
– Endotoxin: ≤0.5 EU/mg (LAL assay; lot-specific)

REGULATORY STATUS

KPV was not placed on FDA Category 2 during the 2023–2024 503A peptide review process — distinguishing it from CJC-1295, ipamorelin, sermorelin, and BPC-157, all of which were placed on (and subsequently removed from) the interim Category 2 list. KPV is not federally scheduled as a controlled substance in the United States. KPV is not on the WADA Prohibited List. Standard research-peptide state-level shipping restrictions apply.

EVIDENCE-DENSITY NOTE (honest disclosure)

KPV’s 2024–2026 primary-literature surface is small relative to BPC-157 or GHK-Cu. The compound has a robust pre-2020 mechanism literature base (NF-κB inhibition, anti-inflammatory activity in colitis, dermatitis, and arthritis research models) that remains foundational. Artemis Labs frames KPV honestly as an established-mechanism, ongoing-translational-research compound rather than a high-volume novel-research target.

For research use only. Not for human or veterinary use.

Stacks

In published research models, KPV is mechanistically complementary to other small repair-pathway peptides because it operates upstream of inflammatory cytokine production via NF-κB suppression, while BPC-157 acts on downstream repair signalling (VEGFR2-Akt-eNOS, FAK) and GHK-Cu operates through copper-mediated remodelling chemistry (Mavrych 2026, PMID 42021992).

BPC-157 / TB-500 — Direct angiogenic and tissue-repair signalling; mechanistically complementary to KPV’s upstream NF-κB inhibition. Frequently studied alongside KPV in tissue-repair research models.

GHK-Cu — Copper-tripeptide acting through copper-mediated repair signalling. The four-peptide research stack pattern (BPC-157 + TB-500 + KPV + GHK-Cu) is documented in tissue-repair research reviews.

MOTS-c — Mitochondrial-derived peptide acting through bioenergetic pathways. Downstream metabolic complement to KPV’s upstream inflammation-pathway suppression.

No dosing, frequency, route, or human protocol is provided. Stacking commentary is restricted to in-vitro and pre-clinical research-design rationale and mechanism-pathway non-redundancy.

For research use only.