ImmuneCathelicidin antimicrobial peptideCAP-18 fragment

LL-37 (Cathelicidin)

The only human cathelicidin · host-defense peptide · double-edged immunology

LL-37 is the only cathelicidin the human body makes — a 37-amino-acid host-defense peptide (it begins with two leucines, hence 'LL') that is cut from a larger precursor protein called hCAP-18 and released by neutrophils and at skin and mucosal surfaces. It is genuinely important biology, not a fringe compound: it punches holes in the membranes of bacteria, fungi and some viruses, it neutralizes bacterial endotoxin, it recruits and tunes immune cells, and — through a receptor called FPR2 — it helps skin re-grow and new blood vessels form, which is why it shows up in wound-healing research. Its production is also switched on by vitamin D, which is part of why vitamin D status is tied to infection defense. So far, so good. The crucial honesty point is that LL-37 is double-edged. The very same peptide can take the body's own DNA and package it in a way that breaks immune tolerance, switching on a type-I interferon response — and that mechanism is a recognized driver of psoriasis, is involved in the skin disease rosacea, and is implicated in lupus. Whether LL-37 protects or harms depends heavily on its concentration, how it's processed, and the tissue it's in. And despite the marketing of injectable 'LL-37 therapy' for healing and anti-aging, there is essentially no controlled human efficacy data and a real, mechanism-based concern about provoking autoimmunity. The fair framing: real and important immunology, with a genuine dark side and almost no human therapeutic evidence.

The short version

Your immune system has a family of small 'host-defense' peptides — short proteins that act like the body's own broad-spectrum antibiotics. Humans make exactly one cathelicidin, and the active piece of it is called LL-37. It's stored in an inactive precursor (hCAP-18) inside neutrophils and skin cells, then snipped out to its active 37-amino-acid form when needed.

What LL-37 does is genuinely impressive on paper. Being positively charged and shaped like a little helix, it is drawn to the negatively charged membranes of bacteria and fungi and tears them open. It also mops up bacterial endotoxin (a molecule that drives sepsis-like inflammation), calls in and coordinates immune cells, and — by activating a receptor called FPR2 — encourages skin to heal and new blood vessels to grow. Its production is turned up by vitamin D, which helps explain the link between vitamin D and infection resistance.

Here is the part the marketing leaves out. LL-37 is double-edged. Under the wrong conditions it grabs onto fragments of the body's OWN DNA and packages them so that immune sensors — which normally ignore self-DNA — suddenly react to it, triggering an inflammatory 'interferon' alarm. That exact mechanism is a well-established driver of psoriasis, plays a role in the skin disease rosacea, and is tied to lupus. So the same molecule that defends you can, in the wrong context, help drive autoimmune and inflammatory disease. Whether it helps or harms depends on how much there is, how it's processed, and where. Add to this that injectable 'LL-37 therapy' for healing or anti-aging has essentially no controlled human evidence behind it, and the cautious read is clear: important immunology, real theoretical risk, very little human proof.

Molecular identity

Specs

Molecular formula: C₂₀₅H₃₄₀N₆₀O₅₃
Molecular weight: ~4493 g/mol (average)
Monoisotopic mass: 4490.5754 Da
PubChem CID: 16198951
UniProt: P49913
CAS / UNII: 154947-66-7 · 3DD771JO2H

Sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES (37 aa)UniProt P49913 (precursor residues 134–170)
Class: Cationic, amphipathic α-helical host-defense (antimicrobial) peptideUniProt P49913; cathelicidin literature
Gene / precursor: Gene CAMP; cleaved from hCAP-18 (cathelicidin antimicrobial peptide precursor, 170 aa)UniProt P49913
INN: RopocamptidePubChem CID 16198951 (INN synonym)
Receptor / mechanism: Membrane disruption (antimicrobial); FPR2/FPRL1 signaling (chemotaxis, wound healing, angiogenesis); LPS neutralization; TLR modulationUniProt P49913; PMID 12782669; PMID 17805349
Plasma half-life: Not established (no human PK; rapidly cleaved by serum/tissue proteases — minutes in vitro)Research literature
Regulatory status: Not an approved drug; research-grade. No controlled human efficacy trials for therapeutic useNo LL-37 drug approval on record

Plain English

Mechanism

LL-37 is a cationic (positively charged), amphipathic peptide that folds into an α-helix. The positive charge draws it to the negatively charged surfaces of microbial membranes, where it inserts and permeabilizes them — killing bacteria, fungi and enveloped viruses by physically disrupting the membrane rather than by hitting a single molecular target. That broad, membrane-level mechanism is why resistance to it is harder to evolve than resistance to conventional antibiotics.

Beyond direct killing, LL-37 is strongly immunomodulatory. It binds and neutralizes bacterial lipopolysaccharide (LPS, or endotoxin), dampening the TLR4-driven inflammatory cascade that endotoxin would otherwise set off. It also recruits and tunes neutrophils, monocytes and T cells, and modulates Toll-like-receptor signaling. A major part of its tissue effects run through the formyl peptide receptor 2 (FPR2, also called FPRL1): activating FPR2 drives cell chemotaxis, keratinocyte (skin-cell) migration and angiogenesis (new blood-vessel formation), which underpins its wound-healing and re-epithelialization activity. The CAMP gene that encodes it is a direct target of the vitamin D receptor, so vitamin D raises cathelicidin levels.

The same chemistry that makes LL-37 useful also makes it dangerous in the wrong setting. Because it binds nucleic acids, LL-37 can complex with self-DNA released from dying cells and ferry it into plasmacytoid dendritic cells, where it activates the intracellular sensor TLR9 and triggers a type-I interferon response. Normally the immune system ignores the body's own DNA; LL-37 breaks that tolerance. This is the mechanistic root of its role in psoriasis and the broader autoimmune concern. Whether LL-37 is protective or pathogenic is therefore context-dependent — a function of concentration, how the peptide is processed by tissue proteases, and the local environment.

Sources:PMID 12782669 PMID 17805349 PMID 17873860

Why people reach for it

Potential benefits

LL-37 is real, important immunology — and a genuinely double-edged molecule. Here's what draws people to it, with the catch that its dark side and the near-absence of human evidence are part of the honest picture, not a footnote.

The body's own broad-spectrum host defense — LL-37 is the only human cathelicidin — it punches holes in the membranes of bacteria, fungi, and some viruses and neutralizes bacterial endotoxin, which is why it's studied as a host-defense peptide.
A wound-healing and angiogenesis signal — Through the FPR2 receptor it drives skin-cell migration and new blood-vessel formation in lab and animal models — the basis for its wound-healing reputation, shown in skin models rather than human trials.
Tied to vitamin D and infection resistance — Its gene (CAMP) is switched on directly by vitamin D, which is part of why vitamin D status is linked to infection defense — and why raising your own LL-37 through vitamin D is the lowest-risk way to engage this biology.
An immune-tuning, not just antimicrobial, role — Beyond killing microbes it recruits and modulates immune cells and dampens TLR4-driven inflammation from endotoxin — a genuinely multi-functional innate-immune signal.

Sources:PMID 12782669 PMID 17805349 PMID 15985530

What people reach for LL-37 for, drawn from what the research reports and how it's used — not proven outcomes or medical claims. The decisive caveat: LL-37 is double-edged — by binding self-DNA it is an established driver of psoriasis, is involved in rosacea, and is implicated in lupus, and injectable LL-37 has essentially no controlled human efficacy or safety data.

Implied timing

Best time to dose

Implied best time

Anytime (consistent)

When used at all, LL-37 is taken at a consistent daily time — it's an innate-immune/antimicrobial peptide with no time-locked action, so the hour doesn't matter the way the dose ceiling and the autoimmune caution do.

LL-37's roles — membrane-level antimicrobial action, FPR2-driven wound signaling, immune tuning — aren't processes that peak at a particular time of day, so no clock window is mechanistically favored.
There is no human pharmacokinetic data (it's cleaved by serum proteases within minutes in vitro), so there's nothing to time a dose around; a consistent daily slot is simply the practical default for adherence.
For this molecule the timing question is far less important than the dose and cycle ceiling: the double-edged autoimmune risk means keeping doses low and cycles short matters much more than what hour you inject.

No study establishes an ideal time of day for LL-37 — this is reasoned from its mechanism and how it's used. As a rule of thumb most peptide dosing lands in the midday-to-evening window; for LL-37 any consistent time is fine, and the real attention belongs on dose, cycle length, and the autoimmune caution.

How to run it

Dosing & protocol

LL-37 is dosed here as a subcutaneous injection — the research-peptide form the calculator serves. There is NO established human dose and no human clinical trial to draw one from. The ranges and schedule below are community convention, assembled from practitioner discussion and the double-edged biology itself. Read every number as a usage pattern, not a validated prescription — and read the frame line below before acting on any of it.

DOUBLE-EDGED CAUTION: LL-37 has no human efficacy trials and no published human dose. More is not better — this peptide is a documented driver of psoriasis, rosacea and lupus-type autoimmune biology when dysregulated. Convention doses exist; a human safety ceiling does not.

Dose — no established human dose

Because no human trial has ever tested a therapeutic LL-37 dose, every number here is community convention framed as such — not evidence.

Convention low:: ~500 mcg once daily subcutaneously — the lower end of community convention, chosen to minimize the autoimmune risk inherent to this molecule.
Convention mid:: ~1,000 mcg (1 mg) once daily subcutaneously — the midpoint most often cited in practitioner forums for wound-healing and angiogenic goals.
Route:: Subcutaneous (SubQ) injection into abdominal fat or outer thigh. The body's own LL-37 is produced and acts locally; systemic subcutaneous delivery is therefore a departure from physiology, not an established route.
Double-edged floor:: Given the mechanistic link between elevated LL-37 and autoimmune flares (psoriasis, rosacea, lupus), many practitioners keep doses at the low end of convention or skip the peptide entirely if any autoimmune history is present.

Subcutaneous administration

Inject into subcutaneous fat — site rotation and timing are the actionable variables.

Injection site:: The abdomen (staying a couple of inches clear of the navel), outer thigh, or love-handle area. Rotate sites between doses to prevent local irritation and lipohypertrophy.
Measuring the dose:: Drawn on a U-100 insulin syringe from the reconstituted vial. At the standard mix (10 mg vial + 2 mL BAC water = 5,000 mcg/mL): 500 mcg = 10 IU · 1,000 mcg = 20 IU. The calculator above does this live for any vial size.
Time of day:: No timing data exists, and LL-37 isn't time-locked — a consistent daily slot is all that matters for adherence. See Best time to dose above; for this molecule, dose and cycle length deserve far more attention than the hour.
Food window:: Subcutaneous injection does not compete with food for absorption — inject independent of meals.

Cycle & washout

The double-edged biology argues for shorter cycles and careful monitoring — not indefinite use.

Convention cycle:: 2–4 weeks of daily use, then reassess. The autoimmune risk is the reason for the shorter ceiling here versus most peptides — this is not a molecule to run indefinitely without monitoring inflammatory markers.
Washout:: Follow with a 2–4-week break minimum. During the break, observe for any sign of inflammatory flare (skin changes, joint tenderness, fatigue) — early signals that the double-edged axis may be activating.
Stop criteria:: Stop immediately and do not re-challenge if any psoriatic, rosacea, or lupus-type symptoms appear during or after a cycle. This is a hard stop, not a 'lower the dose' scenario.

Reconstitution at a glance

Mixing math only — the calculator above does this live for any vial and dose:

Standard mix:: 10 mg vial + 2 mL bacteriostatic water = 5,000 mcg per mL. On a U-100 insulin syringe: 500 mcg = 10 IU · 750 mcg = 15 IU · 1,000 mcg = 20 IU.
Why 2 mL for LL-37:: The calculator defaults use 2 mL for this vial size, keeping the concentration high enough that small convention doses are measurable without microscopic increments.

Sources:PMID 12782669 PMID 17805349 PMID 17873860 PMID 17676051

Substrate the signal needs

Nutritional cofactor precision

LL-37 is antimicrobial, wound-healing, and angiogenic — but also a documented driver of autoimmune inflammation when dysregulated. The useful cofactors amplify the host-defense side through physiology (not more injected peptide), supply the substrates the healing and immune roles consume, and actively mitigate the double-edged risk. Every entry traces to LL-37's specific mechanism.

Reasoned from LL-37's CAMP gene / vitamin-D-receptor axis, FPR2-driven wound biology, and the double-edged self-DNA/TLR9/type-I-IFN mechanism — not an LL-37 cofactor study. Supplement doses are common community ranges. The double-edged warning is not a caveat: it is the central fact about this molecule.

Vitamin D — the on-mechanism amplifier

The CAMP gene that encodes LL-37 is a direct vitamin D receptor (VDR) target. Vitamin D to sufficiency is the single most on-mechanism move available — it raises your own endogenous cathelicidin in its normal, locally regulated context.

Mechanism:: The vitamin D receptor binds directly to the CAMP gene promoter and switches on cathelicidin transcription (Gombart 2005, FASEB J, PMID 15985530). This is established immunology — vitamin D status is a primary dial on your body's own LL-37 production, which is why vitamin D deficiency is consistently linked to impaired host defense and infection susceptibility.
Why this is the headline cofactor:: Raising endogenous LL-37 via vitamin D does it in the controlled, tissue-local way the body evolved — the opposite of flooding the system with injected peptide at uncertain doses. If host-defense support is the goal, fixing a vitamin D deficiency is the most honest, lowest-risk intervention.
Protocol integration:: Vitamin D3 dosed to a serum 25(OH)D level in the sufficient range (conventionally 40–60 ng/mL). Many protocols use 2,000–5,000 IU/day D3 + 100–200 mcg K2-MK7 to direct calcium appropriately. Get a baseline blood level first — supplementing at high doses without knowing baseline is unnecessary.
Double-edged note:: Optimal vitamin D → optimal (not maximal) cathelicidin. The goal is sufficiency within the physiological range, not driving cathelicidin as high as possible. The same double-edged concern applies: chronically supraphysiological cathelicidin is the autoimmune-risk direction.

Zinc + vitamin C — supply the immune and wound-repair substrate

LL-37 operates at the intersection of host defense and wound repair. Both roles consume specific substrates that are easily depleted — zinc for immune cell function and antimicrobial activity, vitamin C for the collagen remodeling and barrier repair LL-37 helps initiate via FPR2.

Zinc — mechanism:: Zinc is structurally required for immune cell function across neutrophils, macrophages and T cells — the same cells that make and respond to LL-37. Zinc deficiency directly blunts host defense and impairs antimicrobial peptide effectiveness. It also supports skin barrier integrity, the primary tissue LL-37 defends.
Zinc — protocol integration:: 25–40 mg zinc picolinate or bisglycinate daily with food. If running >30 mg for more than 4 weeks, pair with 1–2 mg copper bisglycinate to prevent copper depletion.
Vitamin C — mechanism:: LL-37 drives re-epithelialization and wound closure via FPR2 (Carretero 2008). Collagen synthesis — the structural substrate of that repair — requires vitamin C as a cofactor for prolyl hydroxylase. Depleted vitamin C blunts the repair output LL-37 is signaling for.
Vitamin C — protocol integration:: 500–1,000 mg ascorbic acid or ascorbate (buffered) daily in divided doses; higher end around wound-recovery periods.

Mitigate the double-edged risk — the 'more is not better' protocol

LL-37 is not a one-directional healing compound. Because it can break immune tolerance to self-DNA and drive psoriasis, rosacea and lupus-type biology, the mitigate function is not optional here — it is the most important cofactor category for this molecule.

The risk mechanism:: LL-37 binds self-DNA released from dying cells and ferries it into plasmacytoid dendritic cells where it activates TLR9 → type-I interferon response, breaking tolerance. This is not a theoretical risk: it is the established mechanism of psoriasis (Lande 2007, Nature, PMID 17873860) and is implicated in rosacea and lupus. Elevated, dysregulated cathelicidin — exactly what injectable LL-37 aims to produce — is the scenario this mechanism requires.
Omega-3s (EPA/DHA):: EPA and DHA independently dampen TLR-driven and type-I-IFN signaling, pushing the immune environment in the opposite direction from the autoimmune cascade LL-37 can trigger. ~2–3 g combined EPA/DHA daily as a background suppressor of the pro-inflammatory side of LL-37's biology.
Vitamin A (retinol):: Vitamin A modulates skin and mucosal immune tone and is required for regulatory T-cell differentiation — the regulatory arm that typically keeps self-reactive inflammatory responses in check. ~700–900 mcg RAE (retinol equivalents) from food or a modest supplement; megadosing retinol is separately toxic.
Hard stop criteria:: No cofactor offsets a genuine autoimmune flare triggered by LL-37. Any new psoriatic, rosacea, or lupus-type symptoms during a cycle are a stop-immediately signal, not a 'reduce and continue' one. Pre-existing autoimmune or inflammatory skin conditions are a contraindication to LL-37, not a cofactor optimization problem.

Combinations + timing

Stacking notes + timing windows

LL-37's strongest preclinical roles are antimicrobial host defense, wound-healing re-epithelialization, and angiogenesis (new blood-vessel formation via FPR2). The best pairings bring a complementary repair or structural-rebuild lever to that angiogenic/healing signal — not another immune activator, which would push the double-edged risk in the wrong direction. The caution for LL-37 stacking is stronger than for most peptides: because it can drive autoimmune inflammation, combining it with other immune stimulators is exactly the wrong direction.

User combinations reasoned from complementary mechanisms — not regimens studied head-to-head. LL-37 itself has no human efficacy trial, so any stack is doubly unproven. The double-edged autoimmune risk is the dominant fact about LL-37 stacking — it is not a minor footnote.

LL-37 + BPC-157

LL-37 brings the antimicrobial environment and the angiogenic signal; BPC-157 brings the structural repair. Different levers, not the same one twice.

Why it works:: LL-37's FPR2-driven angiogenesis (Koczulla 2003) seeds the wound with new blood supply; BPC-157 is studied for tendon, gut-lining, and connective-tissue repair downstream of that blood supply. LL-37 handles the host-defense and neovascularization phase; BPC-157 handles the structural rebuild — complementary roles in wound progression.
The protocol:: LL-37 ~500–1,000 mcg SubQ daily + BPC-157 250–500 mcg SubQ daily, rotated injection sites across the week. Given LL-37's shorter conventional cycle (2–4 weeks), it leads the stack; BPC-157 can continue through a washout if the repair goal is still active.
Outcome:: The combination users reach for on wound-healing, post-surgical recovery, and tissue-repair goals where both host defense and structural rebuild are relevant. Reasoned, not studied — and the LL-37 double-edged caveat applies in full.

LL-37 + BPC-157 + TB-500

Adds TB-500's cell-migration and actin-remodeling signal to the LL-37 angiogenesis + BPC-157 structural rebuild — three distinct jobs in wound recovery.

Why it works:: TB-500 (Thymosin β4) promotes the migration of repair cells into injured tissue and modulates actin polymerization for cytoskeletal remodeling — the cellular-movement phase of repair. BPC-157 handles structural matrix rebuild; LL-37 handles angiogenesis and the antimicrobial environment. Three distinct mechanistic levers on the same wound, none redundant.
The protocol:: LL-37 ~500–1,000 mcg SubQ daily (2–4-week cycle) + BPC-157 250–500 mcg SubQ daily + TB-500 on its own loading schedule (typically 2–4 mg/week loading for 4 weeks, then 500 mcg–2 mg/week maintenance). LL-37's cycle ends first; the BPC-157 + TB-500 pair can continue through the washout.
Outcome:: The recovery trio users reach for on significant soft-tissue injury, post-surgical recovery, or chronic wound contexts. Reasoned from three distinct mechanisms, not studied. LL-37's autoimmune double-edge applies in full — this stack is not for anyone with an inflammatory or autoimmune predisposition.

Reconstitution math

Reconstitution calculator

Calculated for a 1 mL U-100 insulin syringe (100 units/mL).

Peptide per vial

BAC water added

Desired dose

Units per dose

Draw to this mark on a U-100 syringe

Volume per dose: 0.2 mL
Doses per vial: 10
Concentration: 5 mg/mL

One vial lasts

Daily: 10 days
Every other day: 20 days
5×/week: 14 days

Research use only. Not for human consumption. Outputs are reference values based on research literature — verify all measurements independently.

From the studies

Side effects from research

The defining safety concern for LL-37 is not a typical injection side effect — it is the molecule's documented capacity to drive autoimmune and inflammatory disease. By binding self-DNA and activating plasmacytoid dendritic cells through TLR9, LL-37 can break the immune system's tolerance to the body's own DNA and trigger a type-I interferon response. This mechanism is an established driver of psoriasis, is involved in rosacea (via abnormal cathelicidin processing), and is implicated in lupus. That is a mechanism-based, not hypothetical, reason for caution.

Beyond that, there is essentially no controlled human safety data for LL-37 used as a therapeutic. There are no large trials, no long-term surveillance, and no established dose — so the ordinary risks of an unapproved injectable (purity, identity, contamination from gray-market sourcing; local injection-site reactions) sit on top of the deeper biological concern.

The honest summary: LL-37 is not a benign 'healing' peptide. It is a context-dependent immune molecule that can be protective or pathogenic, with a real and specific link to autoimmune skin and systemic disease, and almost no human evidence to characterize its safety as a supplement or therapy.

Sources:PMID 17873860 PMID 17676051

As reported in literature

Research dosing ranges

There is no human dose for LL-37 — the table below is preclinical (in-vitro, animal, ex-vivo human skin) and is shown to illustrate the mechanism, not to suggest a regimen. Read it for the double-edged story: the same peptide that is antimicrobial, wound-healing and angiogenic also breaks tolerance to self-DNA and drives psoriasis and rosacea. No milligram or microgram dose is given because none is established.

Dose	Route	Model	Outcome	Sources:
In vitro / animal	Local / experimental	Angiogenesis & FPRL1 signaling (Koczulla 2003, J Clin Invest)	LL-37/hCAP-18 is angiogenic — promotes new blood-vessel formation via the FPRL1 (FPR2) receptor, linking host defense to neovascularization	PMID 12782669
In vitro / in vivo (skin)	Topical / local	Wound healing (Carretero 2008, J Invest Dermatol)	LL-37 promotes re-epithelialization and wound closure — a basis for its wound-healing reputation, shown in skin models rather than human trials	PMID 17805349
Cellular / molecular	Experimental	Self-DNA / pDC / TLR9 axis (Lande 2007, Nature)	DOUBLE-EDGED: LL-37 binds self-DNA, forms complexes that activate plasmacytoid dendritic cells via TLR9 → type-I interferon, breaking immune tolerance — a driver of psoriasis	PMID 17873860
Animal / mechanistic	Local	Cathelicidin processing in rosacea (Yamasaki 2007, Nat Med)	DOUBLE-EDGED: abnormal protease (KLK5) processing of cathelicidin generates inflammatory peptide forms that drive rosacea skin inflammation	PMID 17676051

Quick answers

Frequently asked

What is LL-37, exactly?

It's the only cathelicidin the human body makes — a 37-amino-acid host-defense peptide cut from a precursor protein (hCAP-18) and released by neutrophils and at skin/mucosal surfaces. It kills microbes by disrupting their membranes, neutralizes bacterial endotoxin, tunes the immune response, and helps wounds heal. Its production is switched on by vitamin D.

Is LL-37 safe to take for healing or anti-aging?

There is essentially no controlled human efficacy or safety data for injectable LL-37, and there's a real, mechanism-based concern: LL-37 can break immune tolerance to self-DNA and is an established driver of psoriasis, is involved in rosacea, and is implicated in lupus. It is genuinely double-edged, so the marketing claims run well ahead of the evidence.

Why is LL-37 called 'double-edged'?

The same peptide that defends against microbes and helps wounds heal can, under the wrong conditions, grab the body's own DNA and present it to immune sensors that normally ignore self-DNA — triggering an inflammatory interferon response that drives autoimmune skin disease. Whether it protects or harms depends on concentration, processing, and tissue context.

What dose of LL-37 should I use?

There is no established human dose, and this library does not provide one. The research uses micromolar concentrations in cell culture or local/topical application in animal and skin models — experimental conditions, not human treatment doses. Given the autoimmune concern, the absence of dosing data is itself a safety point.

Is LL-37 banned in sport?

It is not specifically named on the 2026 WADA Prohibited List. As a host-defense/antimicrobial peptide rather than a growth-factor or hormone mimetic, it is likely not prohibited — but WADA's open-ended 'related substances and mimetics' language means non-named peptides can be captured at its discretion. This is an inference, not a verified ruling, so athletes must verify against the official WADA list and their anti-doping authority.

Primary sources

References

PMID 12782669Koczulla et al., J Clin Invest 2003 — LL-37/hCAP-18 is angiogenic via FPRL1 (FPR2); links host defense to neovascularization
PMID 17805349Carretero et al., J Invest Dermatol 2008 — LL-37 promotes wound healing / re-epithelialization
PMID 15985530Gombart et al., FASEB J 2005 — CAMP (cathelicidin) is a direct vitamin-D-receptor target gene
PMID 17873860Lande et al., Nature 2007 — LL-37 binds self-DNA, activates pDCs via TLR9 → type-I IFN; breaks tolerance in psoriasis
PMID 17676051Yamasaki et al., Nat Med 2007 — abnormal cathelicidin (KLK5) processing drives rosacea skin inflammation
PubChem CID 16198951PubChem record — identity (CID, formula, MW)
UniProt P49913UniProt P49913 — cathelicidin antimicrobial peptide (gene CAMP); LL-37 sequence
WADA 2026WADA 2026 Prohibited List — LL-37 not named; classification an inference

Research use only · Not medical advice · Updated 2026-06-01