pe
pep-10909 v1 CC-BY-SA-4.0

KPV: anti-inflammatory gut peptide (Lys-Pro-Val)

A tiny three-amino-acid fragment of the skin hormone alpha-MSH that calms gut inflammation in animal studies; experimental, not yet an approved drug.

statusbioassayed targetMC1R length3 aa refs18
snapshot preclinical 0% confidence
Class
Anti-inflammatory tripeptide; alpha-MSH C-terminal fragment
Status
Not approved by FDA, EMA, or any major regulatory authority. Not an approved medicine in any major jurisdiction. Under active FDA compounding review (PCAC consultation scheduled July 23, 2026).
Best-supported effect
Reduced mucosal inflammation in rodent colitis models (DSS, TNBS, transfer colitis) via direct intracellular NF-κB inhibition; supported by consistent animal-model evidence. In vitro: NF-κB inhibition confirmed across multiple cell types.
Main caveat
No published human efficacy trials for any indication; all clinical claims rest on preclinical and mechanistic evidence only.
status 5 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.310
pTM0.721
avg pLDDT52.5
ranking score0.453
STRUCTURE · PEP-10909 × MC1R
ranking0.453
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence3 aa
13
KPV
in the news 2 articles
overview readme

Snapshot

Class: Anti-inflammatory tripeptide; alpha-MSH C-terminal fragment
Evidence tier: Animal-only evidence
Status: Not approved by FDA, EMA, or any major regulatory authority. Not an approved medicine in any major jurisdiction. Under active FDA compounding review as of April 2026.
Best-supported effect: Reduced mucosal inflammation in rodent colitis models (DSS, TNBS, transfer colitis) via direct intracellular NF-κB inhibition; supported by consistent animal-model evidence
Main caveat: No published human efficacy trials for any indication; all clinical claims rest on preclinical and mechanistic evidence only


What this is

KPV is a tripeptide consisting of three amino acids — lysine, proline, and valine — representing positions 11–13 at the C-terminal end of alpha-melanocyte-stimulating hormone (alpha-MSH). It was identified during systematic dissection of alpha-MSH's activity in the 1980s and 1990s as the minimal sequence retaining substantial anti-inflammatory activity, while lacking the melanocortin receptor-binding sequence responsible for alpha-MSH's pigmentary, appetite, and arousal effects. KPV does not activate MC1R through MC5R and therefore does not produce tanning or other melanocortin-mediated effects. At approximately 342–357 Da (sources differ; see Chemistry), KPV is unusually small for a bioactive peptide and is actively transported across intestinal epithelium via the PepT1 di/tripeptide transporter, providing a mechanistic basis for oral delivery to colonocytes — a property uncommon among peptide drug candidates. Despite several decades of preclinical characterization and a well-characterized mechanism, KPV has not advanced to controlled human clinical trials.


Evidence map

Evidence layerGradeWhat it supports
HumanNone identifiedNo human efficacy trials are present. A 2025 systematic review confirms zero human KPV-specific clinical trials identified in the published literature.
AnimalModerate–StrongReduced inflammation in DSS-induced colitis, TNBS-induced colitis, and CD45RBhi transfer colitis models; reduced inflammatory markers and histologic damage in rodent studies; skin inflammation reduction in contact dermatitis models; colitis-associated cancer reduction in murine models
In vitroModerateNF-κB nuclear translocation inhibition in colonic epithelial cells, macrophages, and keratinocytes; TNF-alpha, IL-6, IL-1beta, and IL-8 reduction; iNOS and nitric oxide suppression; PepT1-mediated uptake confirmed in Caco-2 cells; tight junction protein upregulation; antimicrobial activity against S. aureus (including MRSA) and C. albicans at higher concentrations
ComputationalNot presentNo computational or docking data identified
MechanismStrongNF-κB inhibition via IκB-alpha stabilization is well-characterized across multiple cell types. More recent work (Sung et al. 2025, source-cited) extends the mechanism upstream to ERK/p38 MAPK inhibition and caspase-1 blockade. PepT1-mediated intestinal uptake is mechanistically established. Receptor-independence from melanocortin receptors confirmed.

A large share of the published preclinical evidence traces through a small number of research networks (Merlin/Dalmasso at Emory/Georgia State for gut evidence; Böhm/Brzoska/Luger for skin/immune evidence). Independent replication depth across unaffiliated labs is a consideration for interpreting the evidence base.


Claim check

ClaimVerdictEvidence layerConfidence
Suppresses NF-κB activation and reduces pro-inflammatory cytokinesSupported (in vitro / animal)In vitro, animalHigh — consistent across multiple cell types and colitis models
Reduces intestinal mucosal inflammation in colitis modelsSupported (animal)AnimalHigh — replicated across DSS, TNBS, and transfer colitis models
Effective anti-inflammatory treatment for human IBDNot establishedAnimalHigh — no completed human efficacy trial identified
Effective for human skin inflammatory conditions (eczema, psoriasis, dermatitis)Not establishedIn vitro, animalHigh — preclinical skin models only; no controlled human trial
Orally bioavailable via PepT1 transporterSupported (in vitro / animal)In vitro, animalHigh — PepT1-mediated uptake confirmed in cell and animal models; human pharmacokinetics not characterized
Safer than corticosteroids for chronic inflammationNot establishedIn vitro, animal (mechanistic)High — KPV lacks HPA-axis suppression and steroid-class adverse effects per preclinical data; no head-to-head human comparison exists
Causes tanning or melanocortin-receptor-mediated effectsContradictedIn vitro, animalHigh — KPV lacks the His-Phe-Arg-Trp MC-receptor-binding sequence; MC1R-knockout experiments confirm receptor-independent mechanism

Experimental exposure

This section reports exposure used in animal experiments. It does not establish human dosing.

ContextSystemExperimental exposureDurationEndpointLimitation
DSS colitis modelMice (oral administration)Oral KPV; specific dose not individually extracted from available literatureDays to weeks per model protocolDisease activity score, colonic inflammation markers, mucosal histology, pro-inflammatory cytokine mRNARodent model; human pharmacokinetics and efficacy not established
TNBS colitis modelMice (oral administration)Oral KPV; specific dose not individually extracted from available literatureDays to weeks per model protocolInflammatory scores, mucosal damage, cytokine levelsDifferent induction chemistry from DSS; neither model predicts human efficacy
CD45RBhi transfer colitisMC1R-deficient miceOral KPV; specific dose not individually extractedPer model protocolSurvival, colitis severityMC1R-knockout design confirms non-MCR mechanism; no human translation established
Nanoparticle-enhanced deliveryMice (colitis models)KPV-loaded hyaluronic acid nanoparticlesPer study protocolTargeted colonic delivery; inflammation markersDelivery-system data; no approved formulation exists
Contact dermatitis modelMice (topical application)Topical KPV; concentration not individually extractedPer model protocolEar swelling, inflammatory infiltrateSkin model; no human dermatology trial identified

Preclinical safety signals

SignalSystemNotes
No major toxicity at therapeutic dosesRodent and cell culture modelsSource describes no significant toxicity in preclinical studies even at doses above the therapeutic range; duration of studies and full toxicology details not individually extracted
Absence of melanocortin-mediated effectsCell and animal modelsKPV does not activate MC1R–MC5R; no pigmentation, appetite, or arousal effects expected or observed
Short plasma half-lifeper available sourcesShort plasma half-life described; stable in GI tract per source; formal PK characterization not available
Long-term safetyNot characterizedNo chronic animal toxicology data individually extracted; no human safety data in source
Pregnancy and reproductive safetyNot characterizedNo reproductive toxicology data identified in source

Regulatory status

Region / bodyStatusNotes
United States (FDA)Not approvedNot FDA-approved for any indication. Removed from 503A Category 2 (April 22, 2026) after the nomination was withdrawn. FDA has indicated intent to consult the Pharmacy Compounding Advisory Committee (PCAC) on July 23, 2026 regarding KPV acetate and KPV (free base). Removal from Category 2 does not authorize compounding; KPV remains an unapproved new drug for US compounding purposes until PCAC acts and FDA finalizes. Source: FDA 503A bulk substances document, updated April 22, 2026.
European UnionNot approvedNo EMA authorization identified in source. per available sources as unapproved investigational peptide.
Other major jurisdictionsNot approvedPer available sources, no major regulator (MHRA, TGA, Health Canada) has authorized KPV.
WADANot listed by namePer available sources, KPV is not currently listed by name on the WADA Prohibited List. Source also notes that WADA's S0 catch-all category covers substances not approved by any governmental regulatory health authority for human therapeutic use — a description that applies to KPV. per available sources status; current list has not been independently verified in this card.

Mechanism

KPV's anti-inflammatory mechanism is receptor-independent and intracellular. The peptide crosses cell membranes and enters the cytoplasm, where its primary action is stabilization of the inhibitory IκB-alpha protein that normally sequesters NF-κB in the cytoplasm. By preventing NF-κB nuclear translocation, KPV suppresses transcriptional activation of hundreds of pro-inflammatory genes. Downstream consequences include reduced production of TNF-alpha, IL-6, IL-1beta, IL-8, iNOS, and nitric oxide. More recent work described in the available literature (Sung et al. 2025, Tissue & Cell) extends the mechanism upstream, positioning KPV as a multi-node inhibitor acting on ERK/p38 MAPK signaling and caspase-1 activation in addition to NF-κB. KPV also inhibits inflammasome activation and reduces prostaglandin E2 production per the available literature. This intracellular mechanism is distinct from full-length alpha-MSH, which acts via melanocortin receptors; KPV reaches the same anti-inflammatory downstream state through a receptor-independent intracellular path.

In the gut, PepT1 — a di/tripeptide transporter expressed on intestinal epithelial cells — actively transports KPV intact across the intestinal epithelium. PepT1 expression is upregulated in inflamed intestinal tissue, which may enhance KPV uptake preferentially at inflamed sites. This transport mechanism provides the mechanistic rationale for oral delivery to colonocytes.

Target confidence: The NF-κB/IκB-alpha mechanism is well-established across multiple cell types in available literature literature. The ERK/p38 MAPK and caspase-1 extensions are more recent and not yet as broadly replicated.


Chemistry

FieldValue
SequenceLys-Pro-Val
Length3 amino acids
TopologyLinear
Molecular formulaC₁₆H₃₁N₅O₄
Molecular weight357.4 Da (RP source) / 342.43 g/mol (PE source) — values differ between sources; see note
CAS67727-97-3
ModificationsNone identified; naturally occurring fragment
Salt formKPV (free base) and KPV acetate both mentioned in FDA compounding context
OriginC-terminal fragment (positions 11–13) of alpha-melanocyte-stimulating hormone (alpha-MSH), a 13-amino-acid peptide hormone
Sequence confidenceNeeds review — sequence itself is consistent across sources; molecular weight values differ between source sections

Molecular weight note: One available literature reports 342.43 g/mol; another reports 357.4 Da. These values differ by approximately 15 mass units. The discrepancy may reflect different salt forms (free base vs. acetate) or a source error. Both values are preserved here; verification against primary chemistry data is recommended before relying on either value.


Open questions

  • Human efficacy translation: No completed controlled human trial has tested whether KPV's substantial animal-model effects translate to clinical benefit in IBD, ulcerative colitis, Crohn's disease, or skin inflammation. This is the most important research gap — the distance between mechanistic strength and clinical validation is large.
  • Human pharmacokinetics: PepT1-mediated oral uptake is established in rodent and cell models, but oral bioavailability, distribution, metabolism, and clearance in humans have not been rigorously characterized. Whether KPV reaches the colon at pharmacologically relevant concentrations after oral dosing in humans is unconfirmed.
  • Optimal formulation for gut delivery: Preclinical work has investigated nanoparticle and hydrogel delivery systems as superior to standard capsule delivery for colon-targeting. Whether enteric-coated, standard, or targeted-delivery formulations are required for human colonic efficacy is unresolved.
  • Long-term safety: No chronic safety data is present in available literature for any species or route. Short plasma half-life and tripeptide structure suggest low accumulation, but long-term immunomodulatory effects are uncharacterized.
  • Molecular weight discrepancy: Source sections report 342.43 g/mol and 357.4 Da; verification against a primary chemistry reference is needed.
  • US compounding regulatory outcome: FDA has indicated intent to consult PCAC on July 23, 2026 regarding KPV acetate and KPV (free base). The outcome of this process is pending and will be relevant to legal availability of compounded KPV in the US.
  • Subcutaneous systemic pharmacodynamics: The mechanistic rationale for KPV is strongest for local routes (oral for gut, topical for skin) where direct tissue contact is the mechanism. Whether subcutaneous injection produces meaningful systemic anti-inflammatory exposure at typical doses has not been established.
Hypotheses6 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Is there a way to treat inflammatory bowel disease that leaves the rest of your immune system working normally?

Most IBD drugs suppress immunity everywhere, raising the risk of serious infections. If this hypothesis holds, KPV would concentrate its anti-inflammatory effect in the intestinal lining and leave circulating immune cells untouched, potentially allowing long-term use without the infection risk that limits current therapies.

The hypothesis
KPV selectively inhibits NF-kB in mucosal epithelial cells and tissue macrophages but not in systemic lymphocytes, because PepT1 expression confines intracellular delivery to enterocytes and intestinal macrophages, while circulating immune cells lack PepT1 and exclude KPV, thereby preserving systemic immune surveillance during oral KPV treatment.
Why it’s plausible
PepT1 is expressed at high levels in intestinal epithelium and is upregulated in inflamed mucosa, but is absent or minimal in peripheral blood lymphocytes. If intracellular delivery depends on PepT1-mediated transport (as established in Caco-2 and PepT1-KO mouse data), then oral KPV would concentrate anti-inflammatory activity in the gut mucosa while leaving systemic T and B cell function intact. This stands in sharp contrast to systemic immunosuppressants (corticosteroids, anti-TNF, JAK inhibitors) that impair host defense. A selectivity prediction of this kind is directly falsifiable by comparing NF-kB activation in PepT1-positive vs. PepT1-negative cell types after equivalent KPV exposure.
Why it matters
Confirming mucosal-selective immunosuppression would be a major therapeutic advantage for IBD treatment, potentially enabling continuous use without the infection risk associated with systemic immunosuppression, and differentiating KPV from all current IBD drug classes.
Plausibility.53
Novelty.57
Impact.77
Basis · grounding2 papers · 1 computed/note
[1]
paper
PepT1-dependent mechanism confirmed in colonic tumorigenesis model; PepT1-KO animals lose the KPV effect
doi: 10.1016/j.jcmgh.2016.01.006
[2]
paper
CD44-overexpressing colonic epithelial cells and macrophages identified as primary internalization targets for KPV nanoparticles
doi: 10.1016/j.ymthe.2016.11.020
[3]
notePepT1 actively transports KPV across intestinal epithelium; this property is described as uncommon among peptide drug candidates
openupdated 2026-06-05

Can a small chemical change stop the body from breaking down KPV too quickly before it reaches the gut?

KPV is destroyed rapidly in the digestive tract, which has held back its clinical use. This approach proposes a specific modification that might shield KPV from that degradation while keeping its anti-inflammatory effect intact, which could be a practical step toward a real oral drug.

The hypothesis
N-terminal glycoalkylation of KPV's lysine residue (converting the free amine to a piperidine diol via glucofuranose) increases metabolic stability and oral bioavailability without abolishing NF-kB inhibitory potency, because the Pro-Val C-terminus, not the lysine amine, constitutes the pharmacophoric core for intracellular activity.
Why it’s plausible
The reference doi 10.1371/journal.pone.0199686 describes reductive glycoalkylation of the KPV lysine residue to incorporate the nitrogen into a piperidine diol ring. KPV has a short plasma half-life, likely due in part to rapid aminopeptidase cleavage of the N-terminal lysine. Blocking the lysine amine via glycoalkylation would protect against aminopeptidase degradation while the iminsugar ring bulk may sterically hinder peptidase access. If the Pro-Val C-terminus is the active pharmacophore for IkB-alpha stabilization (Pro-Val conformation constraints are known to confer resistance to carboxypeptidases), then N-terminal modification would preserve activity while substantially extending half-life. The piperidine diol modification also increases aqueous solubility, benefiting formulation.
Why it matters
Half-life extension is the primary engineering bottleneck for KPV clinical translation. A defined structure-activity relationship showing that N-terminal glycoalkylation preserves anti-inflammatory potency would provide a validated prodrug or analog strategy directly compatible with KPV's existing oral delivery via PepT1.
Plausibility.58
Novelty.55
Impact.67
Basis · grounding1 paper · 2 computed/notes
[1]
paper
Reductive glycoalkylation of KPV lysine epsilon-amino group to form piperidine diol derivatives described and synthesized
doi: 10.1371/journal.pone.0199686
[2]
noteShort plasma half-life identified as a pharmacokinetic limitation; formal PK characterization not yet available
[3]
sequenceKPV sequence: lysine at position 1 presents a free amine susceptible to aminopeptidase N cleavage; proline at position 2 provides conformational rigidity protecting the Pro-Val C-terminus
openupdated 2026-06-05

Does KPV work because a gut protein physically carries it inside cells, or because docking onto that protein already sends a signal?

If the transporter itself triggers the anti-inflammatory signal, that would point to a new target for IBD drugs and help explain why KPV's effect is so localized to the colon. It could open a design path for molecules that work on the surface of gut cells without needing to get inside at all.

The hypothesis
PepT1 (SLC15A1) is the functionally relevant molecular target of KPV in colitis, not merely a passive transporter: KPV binding to PepT1 on colonocyte apical membranes directly triggers an intracellular signaling cascade that suppresses NF-kB, such that the anti-inflammatory effect requires PepT1 occupancy and not just cytoplasmic delivery of the intact peptide.
Why it’s plausible
The colitis-associated cancer data (doi 10.1016/j.jcmgh.2016.01.006) shows that PepT1-knockout animals lose KPV protection from tumorigenesis even though a trend toward reduced tumor burden persists, suggesting PepT1 is more than a conduit. PepT1 is a proton-coupled oligopeptide transporter that has been reported to activate MAPK pathways upon ligand binding in non-transport contexts. If KPV's NF-kB inhibition depends on PepT1 occupancy rather than intracellular delivery, then cell-impermeable KPV analogs that bind PepT1 without being transported should still produce anti-inflammatory effects, while transported-but-non-PepT1-binding analogs should not.
Why it matters
If PepT1 is an active signaling receptor for KPV rather than a passive transporter, this would identify a novel signaling axis for IBD therapeutics and explain why KPV's efficacy is tissue-selective (colon, which overexpresses PepT1 during inflammation) rather than systemic.
Plausibility.48
Novelty.68
Impact.72
Basis · grounding2 papers · 1 computed/note
[1]
paper
PepT1-KO animals largely lose KPV protection from AOM/DSS tumorigenesis; the effect is described as PepT1-dependent
doi: 10.1016/j.jcmgh.2016.01.006
[2]
paper
KPV acts as a PepT1 substrate in vitro in Caco2-BBE cells; PepT1-mediated uptake confirmed
doi: 10.1016/j.jcmgh.2016.01.006
[3]
notePepT1-mediated intestinal uptake described as a mechanistic basis for oral delivery to colonocytes
openupdated 2026-06-05

Can a gut peptide limit herpes virus activity in mouth and genital tissue by targeting the host cell's own alarm system?

Acyclovir-resistant herpes strains are a real problem for people with weakened immune systems. If KPV blocks the cell-signaling pathway the virus hijacks to replicate, rather than targeting the virus itself, mutations in the virus would not undermine the treatment, which is a meaningful difference for patients who have run out of antiviral options.

The hypothesis
KPV inhibits HSV-1 mucosal replication in the oral and genital mucosa by suppressing NF-kB-dependent viral gene transactivation rather than by direct virucidal action, and its antiviral effect in mucosa depends on PepT1 expression levels in epithelial cells.
Why it’s plausible
The axis_hits mechanism chunk (doi 10.1159/000494354) describes antiviral activity for the related KP dipeptide fragment against HSV-1, with a direct viral envelope interaction excluded and an intracellular mechanism inferred. HSV-1 ICP0 and other immediate-early genes require NF-kB co-activation for efficient transcription; NF-kB inhibition by KPV could attenuate the initial viral burst without direct virucidal activity. The oral mucosa and genital epithelium both express PepT1, providing a route for KPV delivery to the site of primary HSV-1 infection. This differs from acyclovir, which targets viral thymidine kinase, and would be effective against acyclovir-resistant strains that retain NF-kB-dependent transcription.
Why it matters
Acyclovir-resistant HSV is a growing clinical problem in immunocompromised patients. An NF-kB-based antiviral mechanism would be mutation-resistant since it targets host rather than viral machinery, and the topical or mucosal delivery route aligns with KPV's established PepT1-dependent uptake.
Plausibility.36
Novelty.63
Impact.52
Basis · grounding1 paper · 2 computed/notes
[1]
paper
Related KP peptide shows HSV-1 inhibitory activity via intracellular mechanism; direct viral envelope interaction excluded, suggesting host-mediated pathway
doi: 10.1159/000494354
[2]
noteKPV inhibits NF-kB nuclear translocation across multiple cell types including keratinocytes, which are the primary target cells for HSV-1 epithelial infection
[3]
notePepT1-mediated uptake confirmed in intestinal epithelium; PepT1 is also expressed in oral and genital mucosal epithelia
openupdated 2026-06-05

Could an anti-inflammatory peptide help stop arteries from calcifying in people with chronic kidney disease?

Calcified arteries are a leading cause of heart attacks and strokes in people with chronic kidney disease, and there is no approved drug to treat it. The standard medications for bone calcification (bisphosphonates) cannot be used safely in kidney patients. If KPV interrupts the inflammatory process that triggers the calcification, it could address a serious unmet need for this population.

The hypothesis
KPV reduces vascular smooth muscle cell calcification by suppressing NF-kB-driven osteogenic transdifferentiation, making it a candidate therapy for medial vascular calcification in chronic kidney disease patients who cannot tolerate bisphosphonates.
Why it’s plausible
One reference title explicitly concerns KPV and RAPA self-assembled nanodrugs for vascular calcification therapy (doi 10.1002/adhm.202402320). Vascular calcification is driven by inflammatory NF-kB signaling that promotes RUNX2 and BMP2 expression, converting smooth muscle cells to osteoblast-like phenotypes. KPV's documented IkB-alpha stabilization would suppress this NF-kB-to-RUNX2 axis. CKD patients have the highest calcification burden but cannot use bisphosphonates due to renal clearance toxicity; an orally absorbed, renally safe NF-kB inhibitor acting locally in the gut-absorbed pool would address an unmet need. The short plasma half-life of KPV actually reduces systemic exposure risk in this fragile patient population.
Why it matters
Vascular calcification is a leading cause of cardiovascular mortality in CKD and has no approved pharmacological treatment. A mechanistically grounded hypothesis linking KPV's NF-kB inhibition to calcification suppression opens a new therapeutic indication supported by at least one published study.
Plausibility.35
Novelty.48
Impact.62
Basis · grounding1 paper · 2 computed/notes
[1]
paper
KPV and rapamycin self-assembled nanodrugs studied for vascular calcification therapy, establishing direct preclinical evidence
doi: 10.1002/adhm.202402320
[2]
noteNF-kB inhibition via IkB-alpha stabilization confirmed as primary mechanism; NF-kB drives osteogenic gene expression in vascular smooth muscle cells
[3]
noteShort plasma half-life described, reducing systemic exposure concerns for chronic administration
openupdated 2026-06-05

Does KPV fight inflammation in two independent ways, or does it only work through a single mechanism?

If KPV blocks the inflammasome (the molecular spark plug for IL-1 beta) separately from its better-known effect on gene expression, it would act like two drugs in one. That combination might explain why it can work at low doses and could make it worth studying for diseases driven primarily by the inflammasome, such as gout and certain rare fever conditions, beyond bowel disease.

The hypothesis
KPV suppresses NLRP3 inflammasome assembly in intestinal macrophages by blocking caspase-1 autocleavage through direct competition with the caspase-1 pro-domain, a mechanism that is upstream of and independent from its IkB-alpha stabilization activity.
Why it’s plausible
The readme notes that recent work (Sung et al. 2025) extends KPV's mechanism upstream to caspase-1 blockade. NLRP3 inflammasome activation requires caspase-1 for IL-1beta and IL-18 maturation. KPV's Pro-Val C-terminus structurally resembles dipeptide caspase inhibitor scaffolds. If caspase-1 blockade is an independent mechanism rather than a downstream consequence of NF-kB suppression (NF-kB drives NLRP3 transcription), then KPV would suppress both the transcriptional induction and the post-translational activation of IL-1beta, producing a synergistic dual-block. This dual action would distinguish KPV mechanistically from single-node inhibitors such as JAK inhibitors or anti-TNF biologics.
Why it matters
Establishing inflammasome inhibition as a parallel, independent mechanism would explain why KPV achieves anti-inflammatory efficacy at unusually low doses in some colitis models and would justify its potential in NLRP3-driven diseases such as gout, CAPS, and atherosclerosis beyond IBD.
Plausibility.35
Novelty.40
Impact.60
Basis · grounding3 computed/notes
[1]
noteERK/p38 MAPK inhibition and caspase-1 blockade described as upstream extensions of known KPV mechanism per Sung et al. 2025
[2]
noteReduced inflammatory markers including IL-1beta confirmed in rodent colitis models
[3]
sequencePro-Val C-terminal dipeptide resembles structural motifs in known caspase dipeptide inhibitors (e.g., Ac-YVAD-based)
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.30980703234672546 openfold3-mlx
ranking score 0.4529377520084381 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.886global PDE — lower = better
disorder0.122fraction disordered
chain pair ipTM (A, B)0.310interface quality
3-letter notation
Lys-Pro-Val
recipeopenfold3-mlx 0.3.1
parametervalue
modelopenfold3-mlx 0.3.1
weights
hardware
mlx version
python
random seed
msa strategy
diffusion samples1
runtime163s
predicted bymlx@peptide
predicted at2026-05-03
citationbibtex
peptidemodel (2026). KPV: anti-inflammatory gut peptide (Lys-Pro-Val) (pep-10909, v1). PeptideModel. https://peptidemodel.com/card/pep-10909
@peptide{pep10909,
  sequence = {KPV},
  target   = {mc1r},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
clinical trials 0 trials · checked 2026-05-09
0
no registered clinical trials as of 2026-05-09; we'll re-check periodically
references 18 papers
[15] supporting
[17] supporting
discussion no comments
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