LL-37: Antimicrobial Peptide Research Overview

Your body manufactures its own antibiotics. That fact alone should reshape how you think about immune defense. One of the most studied of these natural antibiotics is LL-37 — a peptide your immune cells produce to kill bacteria, fight viruses, break apart fungal cell walls, and even direct the broader immune response. It is the only member of the cathelicidin family found in humans, and researchers have spent the last two decades uncovering just how much it does.

What makes LL-37 remarkable is its versatility. It recruits immune cells to infection sites, helps close wounds, neutralizes bacterial toxins, and disrupts the stubborn biofilms that make chronic infections so difficult to treat. At the same time, when LL-37 levels go wrong — too high, in the wrong place, or processed abnormally — it can drive the inflammation behind conditions like psoriasis and rosacea.

This guide covers the full picture: what LL-37 is, how your body makes it, what the research shows, and what we know about safety, the vitamin D connection, and current regulatory status.

Quick Facts

Property	Detail
Full name	Human cathelicidin antimicrobial peptide LL-37
Precursor protein	hCAP18 (18 kDa human cationic antimicrobial protein)
Length	37 amino acids
Net charge	+6 at physiological pH (11 positive, 5 negative residues)
Structure	Amphipathic alpha-helix
Gene	CAMP (cathelicidin antimicrobial peptide)
Primary producers	Neutrophils, macrophages, epithelial cells (skin, lung, gut)
Key regulators	Vitamin D, inflammatory signaling (TLR pathways)
FDA status	Not approved; Category 2 on FDA's 503A bulks list
Also known as	CAP-18, CAMP, ropocamptide (drug development name)

What Is LL-37?

LL-37 is a small, positively charged peptide and the only cathelicidin expressed in humans. The name comes from its structure: it is 37 amino acids long, and the first two amino acids are both leucine (abbreviated "L"). While other mammals produce multiple cathelicidins, humans rely on this single peptide as a front-line weapon in innate immune defense.

Structurally, LL-37 is an amphipathic alpha-helix — one side of the helix is attracted to water, while the other side is attracted to fat. This dual nature is central to how it works: the water-loving face lets it travel through body fluids, while the fat-loving face lets it bury into microbial membranes and destroy them.

LL-37 starts as a larger, inactive precursor protein called hCAP18 (human cationic antimicrobial protein 18), stored primarily in neutrophil granules until needed. When infection or tissue damage triggers a response, proteinase 3 clips the active LL-37 peptide from hCAP18's C-terminal end.

Beyond direct antimicrobial killing, LL-37 functions as a signaling molecule. It interacts with multiple receptors on immune cells — including FPRL-1 (formyl peptide receptor-like 1), the purinergic receptor P2X7, and EGFR — to recruit immune cells, modulate inflammation, and promote tissue repair.

How Your Body Produces LL-37

LL-37 is not concentrated in one organ. Your body produces it across multiple barrier surfaces — the places where you are most likely to encounter pathogens.

Neutrophils are the primary source. These white blood cells store large quantities of hCAP18 in their secondary granules and release LL-37 at infection sites within minutes of pathogen detection.

Epithelial cells in the skin, lungs, and gastrointestinal tract also produce LL-37. In the skin, keratinocytes use kallikrein proteases (rather than proteinase 3) to process hCAP18. Lung epithelial cells upregulate production when they detect pathogens through Toll-like receptors.

Other producers include macrophages, dendritic cells, NK cells, mast cells, and T cells. Wherever the body encounters the outside world, it stations this peptide for defense.

Two main signals trigger LL-37 production:

Inflammatory signaling — When TLRs on immune cells detect bacterial or viral components, they activate signaling cascades that upregulate the CAMP gene.
Vitamin D signaling — Active vitamin D (1,25-dihydroxyvitamin D) binds to the vitamin D receptor (VDR), which directly induces the CAMP gene. This pathway is so important that inadequate vitamin D levels prevent macrophages from producing LL-37 altogether. (More on this below.)

Mechanism of Action: How LL-37 Works

LL-37 kills microbes primarily by destroying their cell membranes. The positively charged peptide is attracted to the negatively charged surfaces of bacterial cells — specifically, molecules like lipopolysaccharide (LPS) on Gram-negative bacteria and teichoic acid on Gram-positive bacteria. Human cells have a different membrane composition (predominantly neutral phospholipids and cholesterol), which gives LL-37 some selectivity for microbial targets.

Once LL-37 reaches a bacterial membrane, research shows it works in several ways. At lower concentrations, LL-37 molecules coat the membrane surface like a carpet, thinning it until it collapses. At higher concentrations, they oligomerize into clusters that punch discrete holes through the membrane. Studies on E. coli show that LL-37 perforates both inner and outer membranes, with bacterial death typically occurring within minutes.

But membrane disruption is only part of the story. LL-37 also neutralizes endotoxins by binding LPS, recruits neutrophils, monocytes, and T cells to infection sites, activates immune pathways by stimulating IL-1-beta secretion, and promotes wound closure through EGFR transactivation.

Antibacterial Research

LL-37 shows broad-spectrum antibacterial activity in laboratory studies against Gram-negative bacteria (E. coli, Pseudomonas aeruginosa, Klebsiella pneumoniae), Gram-positive bacteria (Staphylococcus aureus, including MRSA), and Mycobacterium tuberculosis.

Because it attacks membranes through physical disruption rather than targeting specific molecular pathways, bacteria have a much harder time developing resistance to LL-37 compared to conventional antibiotics. It also produces synergistic effects when paired with beta-lactams, glycopeptides, or peptide antibiotics.

However, LL-37's antibacterial activity decreases in physiological salt concentrations and serum — a gap between lab potency and real-world conditions that remains a challenge for therapeutic development.

Antiviral Research

LL-37 demonstrates antiviral activity against a surprisingly wide range of viruses, primarily by disrupting viral envelopes — the lipid membranes that surround many viruses.

Influenza: A landmark study published in PLOS ONE showed that LL-37 reduced disease severity and viral replication in influenza-infected mice to a degree similar to zanamivir (Relenza), an FDA-approved antiviral drug. The peptide appeared to act directly on the virus particles rather than through host cell receptors. Treated mice also had lower levels of pro-inflammatory cytokines in their lungs — suggesting LL-37 might reduce the dangerous "cytokine storm" associated with severe influenza.

Herpes viruses: Research demonstrated that LL-37 significantly decreased the ability of Kaposi's sarcoma-associated herpesvirus (KSHV) to infect oral epithelial cells. The effect was dose-dependent and structure-dependent, with LL-37 disrupting the viral envelope itself rather than affecting host cells.

Broader viral activity: Laboratory studies have documented LL-37 activity against dengue virus, hepatitis C, HIV, RSV, vaccinia virus, and herpes simplex virus type 1. The mechanism appears consistent: LL-37 integrates into viral lipid envelopes, modifies their curvature, and separates the envelope from the nucleocapsid. No human clinical trials for antiviral applications have been completed.

Antifungal Research

Fungal infections have become an increasingly serious clinical problem, particularly in immunocompromised patients. LL-37 shows activity against several Candida species, the most common cause of invasive fungal infections.

Against Candida albicans, LL-37 reduced cell adhesion by 60-80% — significantly outperforming other antimicrobial peptides like histatin 5 and human beta-defensin 3, which only reduced adhesion by 10-30%.

Against the emerging multidrug-resistant pathogen Candida auris, LL-37 showed 100% synergy with amphotericin B and caspofungin, and 70% synergy with fluconazole when tested in combination. These combinations reduced the effective dose of both the antifungal drugs and the peptide by 4- to 8-fold — potentially lowering toxicity while maintaining effectiveness. The mechanism involved membrane permeabilization, oxidative stress induction, and cell cycle arrest.

That said, C. albicans has evolved countermeasures. It secretes aspartic proteases (SAPs) that break down LL-37, gradually reducing its antifungal activity — a reminder that host-pathogen interactions are always a two-way street.

Anti-Biofilm Properties

Biofilms are communities of bacteria encased in a protective matrix that makes them up to 1,000 times more resistant to antibiotics than free-floating (planktonic) bacteria. They are responsible for chronic wound infections, implant-associated infections, and persistent urinary tract infections.

LL-37 can inhibit biofilm formation and break apart established biofilms in laboratory studies. This is particularly relevant for chronic wounds: diabetic foot ulcers, for example, are frequently infected by multiple species of biofilm-forming bacteria, and eliminating the biofilm is often the turning point for healing.

The combination of anti-biofilm and wound-healing properties gives LL-37 a theoretical advantage over conventional antibiotics for treating chronically infected wounds — it addresses both the infection and the tissue repair simultaneously.

Immune Modulation: The Double-Edged Sword

LL-37 does not just kill pathogens directly — it orchestrates the broader immune response. This immunomodulatory role is one of the most actively researched aspects of the peptide, and it reveals a complex picture.

Pro-Inflammatory Effects

LL-37 can amplify immune responses when the body needs to fight harder:

It attracts neutrophils, monocytes, and T cells to infection sites through FPRL-1 receptor signaling
It stimulates IL-1-beta secretion from monocytes by activating the P2X7 receptor
It pushes macrophage development toward the M1 (pro-inflammatory) phenotype, upregulating IL-12p40 while downregulating the anti-inflammatory cytokine IL-10
It bridges innate and adaptive immunity by promoting antigen presentation and dendritic cell activation

Anti-Inflammatory Effects

LL-37 can also dampen excessive inflammation. It neutralizes LPS (preventing endotoxin-driven septic shock), antagonizes pro-inflammatory cytokines including IFN-gamma, TNF-alpha, and IL-12, and blocks Gram-negative bacterial signaling through TLR4.

Whether LL-37 acts as a pro- or anti-inflammatory signal depends on the tissue, concentration, and surrounding immune environment. This dual nature makes it a fine-tuning tool for immune response — powerful, but potentially problematic when regulation goes awry.

For a broader look at peptides that influence immune function, see our guide to Thymosin Alpha-1, which takes a different approach to immune modulation by primarily activating dendritic cells and T lymphocytes.

Wound Healing Research and Clinical Trials

LL-37 promotes wound healing through multiple mechanisms: it stimulates cell proliferation and migration via EGFR transactivation, promotes angiogenesis (new blood vessel formation), and modulates the inflammatory environment at the wound site.

Clinical Trial Evidence

LL-37 (under the development name ropocamptide) has been tested in two randomized, placebo-controlled clinical trials for hard-to-heal venous leg ulcers:

Phase I/II trial (Gronberg et al., 2014): Thirty-four patients received twice-weekly topical applications of LL-37 at 0.5, 1.6, or 3.2 mg/mL, or placebo, for four weeks. The two lower doses showed significant improvement: the 0.5 mg/mL group had a healing rate six times faster than placebo, with a 68% reduction in ulcer area. The 1.6 mg/mL group showed a threefold improvement and 50% area reduction. The highest dose (3.2 mg/mL) did not outperform placebo — suggesting more is not always better with this peptide.

Phase IIb HEAL trial (Mahlapuu et al., 2021): This larger study of 148 patients tested 0.5 and 1.6 mg/mL LL-37 alongside compression therapy. Overall results were mixed — LL-37 did not show statistically significant improvement over placebo across all patients. However, a subgroup of patients with larger wounds (over 10 cm-squared) saw real benefits: 62% on the 0.5 mg/mL dose achieved at least 50% wound closure versus 33% on placebo. The treatment was well tolerated with no drug-related serious adverse events.

These trials represent some of the only controlled human data for LL-37 and, combined with its preclinical evidence, position it as a candidate worth watching in wound care. For other peptides studied in wound healing, see our profiles on BPC-157 and TB-500, both of which have their own mechanisms for promoting tissue repair.

Sepsis Research

Sepsis — a life-threatening overreaction to infection — kills hundreds of thousands of people annually. LL-37 has shown protective effects in multiple animal models.

In a rat model of Gram-negative sepsis, LL-37 reduced lethality to a level comparable to imipenem (a powerful hospital antibiotic) and polymyxin B, while lowering plasma endotoxin and TNF-alpha levels more effectively than conventional antibiotics alone.

In murine sepsis models, researchers identified three protective mechanisms: suppressing macrophage pyroptosis (an inflammatory form of cell death), inducing neutrophil extracellular traps (NETs) that capture and kill bacteria, and stimulating antimicrobial microvesicle release from neutrophils. More recent work shows LL-37 also protects against sepsis-induced lung injury by reducing oxidative damage in alveolar epithelial cells.

Cancer Research: A Complicated Story

If there is one area where LL-37 research gets genuinely confusing, it is cancer. The same peptide can either fight tumors or promote them, depending entirely on the tissue involved.

Where LL-37 Appears to Fight Cancer

Gastric cancer: LL-37 inhibits proteasomal activity, upregulates BMP4 (bone morphogenetic protein 4), and arrests the cell cycle, suppressing tumor growth
Colon cancer: LL-37 and its fragments show anti-proliferative effects; immobilizing LL-37 on magnetic nanoparticles significantly increases its antitumor activity
Pancreatic cancer: LL-37 inhibited tumor growth both in vitro and in vivo by inducing DNA damage, cell cycle arrest through reactive oxygen species (ROS), and reshaping the tumor immune environment by reducing immunosuppressive cells while increasing CD4+ and CD8+ T cells

Where LL-37 May Promote Cancer

Ovarian cancer: LL-37 overexpression promotes tumor progression by recruiting bone marrow-derived stromal cells to the tumor
Breast and lung cancer: LL-37 promotes proliferation and metastasis through ErbB-mediated signaling pathways
Prostate cancer: Reducing LL-37 levels decreased tumor proliferation and invasive potential in both lab and animal studies
Liver cancer: LL-37 promoted hepatocellular carcinoma cell proliferation by activating the PI3K/Akt pathway through EGFR/HER2 phosphorylation

The leading hypothesis for these tissue-specific differences is that different cancer types express different receptors, and LL-37's effects depend on which receptors it activates in a given tissue. This is one reason researchers caution against viewing LL-37 as a simple "anti-cancer" peptide.

The Vitamin D Connection

One of the most clinically relevant discoveries about LL-37 is its tight link to vitamin D. Unlike most antimicrobial peptide genes, the human CAMP gene is primarily regulated by the vitamin D receptor (VDR).

The pathway works like this: immune cells detect a pathogen through Toll-like receptors, which triggers them to convert circulating 25-hydroxyvitamin D (the storage form) into active 1,25-dihydroxyvitamin D. This active form binds to the VDR, directly turning on the CAMP gene and leading to LL-37 production.

The practical implication is stark: if your vitamin D levels are too low, your macrophages cannot produce adequate LL-37. This connection helped explain the long-observed link between vitamin D deficiency and increased susceptibility to infections, particularly tuberculosis. A study of patients with active pulmonary TB found that higher vitamin D levels correlated with higher LL-37 levels and better outcomes.

Researchers have also explored combined approaches: one human study found that 5,000 IU of daily vitamin D3 plus 500 mg of phenylbutyrate twice daily synergistically induced cathelicidin expression, suggesting a potential adjunct therapy for lung infections.

This vitamin D-LL-37 axis is unique to humans and primates. Other mammals do not rely on vitamin D to regulate cathelicidin, which is why mouse studies do not always translate cleanly to human biology.

LL-37 in Skin Diseases

While LL-37's antimicrobial role in the skin is protective, abnormal LL-37 levels or processing contribute to several inflammatory skin conditions.

Psoriasis: LL-37 is strongly overexpressed in psoriatic plaques. Research identified it as a trigger for the autoimmune cascade in psoriasis: LL-37 forms complexes with self-DNA fragments, and these complexes activate plasmacytoid dendritic cells through TLR9 — driving the characteristic inflammatory cycle. LL-37 has also been identified as a T-cell autoantigen in psoriasis, meaning the immune system can mount a direct attack against it.

Rosacea: In rosacea, the problem is abnormal processing. Increased protease activity — possibly driven by Demodex mite colonization — cleaves cathelicidin into unusual fragments that trigger inflammation and erythema. Recent research showed LL-37 directly binds TLR2 on mast cells, triggering degranulation through the TLR2/JAK2/STAT3 axis.

Atopic dermatitis: This condition features a relative deficiency of LL-37, which may partly explain the increased susceptibility to skin infections (particularly S. aureus) seen in affected skin.

For more on peptides with skin-related research, see our profile on GHK-Cu, which has a well-studied role in skin remodeling and repair through different mechanisms.

Safety Profile and Side Effects

LL-37's safety profile is nuanced and dose-dependent. Understanding both the benefits and risks requires looking at several levels of evidence.

Cytotoxicity Concerns

At high concentrations, LL-37 is toxic to human cells. It can reduce viability and promote cell death (apoptosis) in osteoblasts, vascular smooth muscle cells, neutrophils, airway epithelial cells, and T cells. It also shows hemolytic activity — the ability to damage red blood cells — at elevated doses.

In animal studies, low doses (100 micrograms per kilogram) of LL-37 showed no observable toxicity in neonatal rats. High doses (3,000 micrograms per kilogram) caused adverse effects and appeared toxic to organs affected by sepsis.

Autoimmune Considerations

LL-37 can form complexes with self-DNA that stimulate plasmacytoid dendritic cells to produce type I interferon, potentially worsening autoimmune conditions including systemic lupus erythematosus (SLE), rheumatoid arthritis, and atherosclerosis. People with existing autoimmune conditions face higher theoretical risk from exogenous LL-37.

Clinical Trial Safety Data

In the venous leg ulcer trials, topically applied LL-37 was well tolerated with a low occurrence of side effects. In a small COVID-19 study using orally delivered LL-37 (via genetically modified Lactococcus lactis), participants reported no adverse reactions.

Stability Limitations

LL-37 is vulnerable to proteolytic degradation and shows reduced activity in physiological salt concentrations. These limitations have pushed researchers toward shorter, more stable derivatives like GF-17 and P60.4 that retain antimicrobial activity with reduced cytotoxicity.

Dosing in Research Settings

Clinical dosing data for LL-37 comes primarily from topical wound healing studies.

Topical (clinical trial data): 0.5 to 1.6 mg/mL applied twice weekly for four weeks in venous leg ulcer trials. The 0.5 mg/mL dose showed the strongest results, with healing rates six times faster than placebo. A diabetic foot ulcer study used LL-37 cream on a similar schedule with trends toward improved tissue formation.

Preclinical (animal data): Rats tolerated up to 1 mg/kg daily; mice up to 5 mg/kg daily, with protective effects against sepsis at these doses.

Important note: No standardized subcutaneous dosing protocol exists for LL-37 in humans based on controlled clinical data. Subcutaneous dosing information found online is largely anecdotal. Any use remains experimental and should only occur under medical supervision.

Legal and Regulatory Status

LL-37's regulatory status has tightened significantly since 2023.

FDA classification: In September 2023, the FDA placed cathelicidin LL-37 on the Category 2 list of the interim 503A bulk drug substances — the category for substances that "raise significant safety concerns." It was not among the peptides removed from Category 2 in September 2024. The FDA's stated concerns include potential negative effects on male fertility and protumorigenic effects in some tissues.

What this means practically: LL-37 cannot be legally compounded by pharmacies for human use, is not FDA-approved for any indication, has no USP monograph, and products labeled "research use only" are not legal for human therapeutic use.

Drug development: Promore Pharma AB has developed LL-37 under the name ropocamptide for topical wound healing, with Phase IIb trial data published — the most advanced regulatory pathway for this peptide.

For comparison, Thymosin Alpha-1 has a more established regulatory history, with approved pharmaceutical products in several countries outside the United States, while Selank has regulatory approval in Russia.

How LL-37 Compares to Other Peptides

LL-37 is unique as a naturally occurring human antimicrobial. Here is how it relates to other well-studied peptides:

Thymosin Alpha-1 — Both modulate immunity, but TA1 works through adaptive immune activation (T cells, dendritic cells) rather than direct microbial killing, and has a more established regulatory history.
TB-500 / Thymosin Beta-4 — Shares wound-healing properties with LL-37 but works through actin-binding and cell migration rather than membrane disruption.
BPC-157 — Another wound-healing peptide derived from gastric juice proteins, working through nitric oxide modulation and growth factor upregulation.
GHK-Cu — Focused on skin remodeling, GHK-Cu stimulates collagen synthesis through copper-dependent enzyme activation — a different approach than LL-37's immune-mediated healing.

Frequently Asked Questions

What does LL-37 stand for?

The name refers to the peptide's structure: it is 37 amino acids long, and the first two amino acids are both leucine (single-letter code "L"). So LL-37 = two leucines + 37 amino acids total.

Is LL-37 the same as cathelicidin?

Almost. The human cathelicidin gene (CAMP) encodes a precursor protein called hCAP18, and LL-37 is the active peptide fragment released when hCAP18 is cleaved. Since LL-37 is the only human cathelicidin, the terms are often used interchangeably.

Can I boost LL-37 levels naturally?

The most evidence-backed approach is ensuring adequate vitamin D levels (generally 30-50 ng/mL of serum 25-hydroxyvitamin D). Active vitamin D directly induces the CAMP gene that encodes LL-37. Exercise, sleep, and zinc status may also support antimicrobial peptide production.

Is LL-37 legal to purchase?

LL-37 can be found labeled "for research use only," but the FDA has placed it on the Category 2 bulks list — meaning it cannot be legally compounded for human therapeutic use. It is not a controlled substance, but its use in humans is not approved.

What are the main risks of LL-37?

Dose-dependent cytotoxicity, potential to worsen autoimmune conditions (SLE, psoriasis), possible negative effects on male fertility, and protumorigenic effects in certain tissues. The therapeutic window between beneficial and harmful doses appears narrow.

How is LL-37 different from antibiotics?

LL-37 kills bacteria by physically disrupting membranes, while most antibiotics target specific molecular pathways. This makes resistance development less likely. LL-37 also has immunomodulatory, wound-healing, and anti-biofilm properties that conventional antibiotics lack.

The Bottom Line

LL-37 is one of the most thoroughly studied antimicrobial peptides in human biology — genuinely multifunctional, capable of killing bacteria, viruses, and fungi while coordinating the immune response and promoting tissue repair.

The clinical evidence, while limited, is real. Topical LL-37 showed measurable wound-healing benefits in controlled trials. Animal studies consistently demonstrate protection against sepsis. The vitamin D connection has practical implications for anyone interested in immune health.

But the research also reveals genuine complexity. LL-37 is not simply a "good" peptide. Its role in psoriasis, rosacea, and certain cancers shows that more is not always better, and that context matters enormously. The FDA's safety concerns — male fertility effects and protumorigenic potential — reflect real findings in the literature, not regulatory overcaution.

For anyone following peptide research, LL-37 is worth understanding because it represents what your body already does to protect itself. The open question is whether we can harness that natural defense therapeutically — and where the line falls between helpful and harmful.

Any decisions about peptide use should involve a qualified healthcare provider who can evaluate individual risk factors and monitor for adverse effects.

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