LL-37

Dosing from the Literature

Published for immune support: nothing; the human doses are topical, on leg and foot ulcers (Grönberg et al., 2014; Mahlapuu et al., 2021; Miranda et al., 2023), apart from one three-patient trial that injected it into skin tumors (ClinicalTrials.gov NCT02225366). Not published: any trial of LL-37 injected under the skin, which is how it is sold.

The figures below come from very different places: the body's own levels, laboratory tests on bacteria, and the human trials. Nothing here is a dose for injecting LL-37: no trial has tested that route.

What It Is

LL-37 is a 37-amino-acid peptide with the sequence LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES, named for the two leucines at its N-terminus and its 37-residue length (Lai & Gallo, 2009; Wang et al., 2014). It is the only cathelicidin the human genome encodes (Mookherjee et al., 2006): horses, cattle, pigs and sheep carry several cathelicidin genes, while humans, rats and mice carry one (Wang et al., 2014). That gene, CAMP, sits on chromosome 3p21.31 and has four exons across about 2 kb (NCBI Gene, 2026).

LL-37 does not exist as such inside the cell. It is produced as the C-terminal cleavage product of a 170-amino-acid prepropeptide called human cationic antimicrobial peptide of 18 kilodaltons (hCAP-18). hCAP-18 contains a signal peptide, the cathelin-like prosequence (cathepsin-L-inhibitor-homologous N-terminal region that gives the family its name), and the mature C-terminal antimicrobial peptide. hCAP-18 is stored intracellularly in inactive form in the secretory granules of neutrophils, monocytes, NK cells, T and B lymphocytes, mast cells, mesenchymal stem cells, mucosal epithelial cells (skin keratinocytes, airway epithelium, GI and genitourinary tracts), and adipocytes. Upon activation, hCAP-18 is exocytosed and cleaved extracellularly: proteinase 3 in neutrophils generates active LL-37; kallikrein 5 (KLK5) in the skin generates LL-37 from keratinocyte-derived hCAP-18; other tissue-specific proteases generate context-specific cleavage variants (KS-30, KR-20, RK-31, and others) that retain partial activity with altered selectivity.

The CAMP gene is unusual among innate-immunity genes in being a direct transcriptional (at the gene-switching level) target of the vitamin D receptor (Gombart, Borregaard, Koeffler. FASEB J 2005;19(9):1067-77). The CAMP promoter contains a vitamin D response element (VDRE), and 1,25-dihydroxyvitamin D3 produces several-fold upregulation of CAMP mRNA in myeloid cells, keratinocytes, and other tissues. This is the mechanistic basis for why vitamin D status affects innate immunity: low serum 25-OH-D ↔ low cathelicidin tone ↔ impaired epithelial barrier defense. The vitamin D / cathelicidin axis explains a substantial portion of the seasonality and ethnic variation in respiratory and skin infection rates.

LL-37 is supplied for research use as a synthetic peptide (synthesis is straightforward — it is a linear 37-mer with no disulfide bonds or unusual modifications). Multiple research-reagent vendors supply it at ≥98% purity. There is no FDA-approved therapeutic LL-37 product; clinical-development efforts have focused on topical formulations for chronic wound healing, leg-ulcer indications, and ophthalmological use.

Mechanism of Action

LL-37 is pleiotropic: besides killing microbes it has been reported to act in chemotaxis, apoptosis, wound healing, immune modulation and cancer metastasis, and the one human cathelicidin gene yields several peptide forms besides LL-37 itself (Wang et al., 2014). Whether it damps inflammation or drives it depends on the setting (Kahlenberg & Kaplan, 2013).

• Amphipathic helix — NMR structures show LL-37 as a long amphipathic helix (residues 2–31) whose hydrophobic and basic faces bind bacterial lipopolysaccharide and anionic phospholipids (Wang et al., 2014).
• Membrane disruption — It kills bacteria mainly by electrostatic attraction to their negatively charged membranes (Kuroda et al., 2015); a crystal structure in membrane mimics shows LL-37 forming oligomers that build channels (Sancho-Vaello et al., 2020).
• Selectivity — Antimicrobial peptides generally damage human cells only at concentrations above those that kill microbes, helped by host membranes’ different lipids and by serum lipoproteins that bind LL-37 (Lai & Gallo, 2009); toxicity to human cells is still one of the limits on making LL-37 a drug (Ridyard & Overhage, 2021).
• Endotoxin binding — LL-37 binds bacterial lipopolysaccharide (Wang et al., 2014) and has protected animals against endotoxemia and sepsis (Mookherjee et al., 2006).
• TLR modulation (immunomodulation) — In human monocytes and blood cells, low concentrations (≤1 μg/mL) damped the response to TLR2, TLR4 and TLR9 agonists, almost completely preventing TNF-α release (Mookherjee et al., J Immunol 2006; PMID 16456005). In psoriatic skin, the same peptide turns self-DNA into a strong inflammatory stimulus (Schauber & Gallo, 2008).
• Chemotaxis and receptors — Antimicrobial peptides act on mammalian receptors to influence chemotaxis, cytokine release and angiogenesis (Lai & Gallo, 2009); the receptors named for LL-37 include FPR2 (FPRL1) and the EGF receptor (Kuroda et al., 2015).
• Wound healing and angiogenesis (new blood vessel growth) — Reviews describe cathelicidin promoting angiogenesis and wound repair in cell and animal studies (Lai & Gallo, 2009; Schauber & Gallo, 2008). On venous leg ulcers, topical LL-37 sped healing in a 34-person trial (Grönberg et al., 2014) and did not in a 148-person one (Mahlapuu et al., 2021).
• Antiviral activity — In lab tests it lowered herpes simplex virus 1 and adenovirus titers (Gordon et al., 2005), and its central helix is needed for activity against HIV-1 and RSV (Wang et al., 2014).
• Anti-biofilm activity — Reviews report activity against bacterial biofilms in lab models (Ridyard & Overhage, 2021; Wang et al., 2014).
• Synergy with antibiotics — In laboratory tests on bacteria, LL-37 has been reported to act together with beta-lactams, peptide antibiotics, glycopeptides and ceragenins, depending on the strain (Ridyard & Overhage, 2021).
• Vitamin D regulation of expression — The CAMP gene’s promoter carries a vitamin D response element, and 1,25-dihydroxyvitamin D3 raised cathelicidin expression in human cell lines and bone-marrow cells (Gombart et al., 2005).

What the Research Shows

About 2,500 PubMed records name LL-37 and about 5,000 name LL-37 or cathelicidin (PubMed, October 2026), across antimicrobial, immunology, skin-disease and cancer research. Almost all of it is laboratory or animal work. The human trials of LL-37 itself are small and topical: 34 people with venous leg ulcers (Grönberg et al., 2014), 148 in a phase 2b trial that found no healing benefit over placebo (Mahlapuu et al., 2021), and 25 with diabetic foot ulcers (Miranda et al., 2023). Major themes:

• Antimicrobial spectrum — Active against gram-positive (S. aureus including MRSA, S. epidermidis, S. pyogenes, S. pneumoniae) and gram-negative (E. coli, P. aeruginosa, K. pneumoniae, A. baumannii) bacteria with typical MICs in the 1–32 μg/mL range; activity preserved against many multidrug-resistant strains where conventional antibiotics fail. Activity against fungi (C. albicans), enveloped viruses (HSV, influenza), and biofilms documented across multiple independent labs (Wang et al. Biochim Biophys Acta 2014; PMID 24463069; Ridyard & Overhage, 2021; PMC8227053).
• Immunomodulation — Mookherjee 2006 (J Immunol; PMID 16456005) characterized LL-37's TLR-modulatory effects; LL-37 suppresses LPS-induced TNF-α (a major inflammatory signaling molecule) release from macrophages while preserving anti-microbial chemotaxis. This bidirectional immunomodulation is the basis for LL-37's interest as both an anti-infective and an immunomodulator.
• Wound healing — Sørensen et al. and subsequent work demonstrated LL-37 expression in keratinocytes during wound healing and accelerated re-epithelialization with topical application in animal wound models. Multiple Phase 1/2 trials of synthetic LL-37 derivatives (Pep637, OP-145) for chronic venous leg ulcers and diabetic foot ulcers have been conducted.
• Inflammatory skin disease — Reinholz, Ruzicka & Schauber 2012 (PMID 22577261) — comprehensive review of LL-37 in atopic dermatitis (low cathelicidin), psoriasis (high cathelicidin / LL-37-self-DNA TLR9 activation driving autoimmunity), and rosacea (abnormal kallikrein 5 processing of hCAP-18 generating pro-inflammatory cleavage variants — PMC3904447). In rosacea, LL-37 dysregulation is now understood as a key pathogenic mechanism, leading to therapeutic interest in tetracyclines (which inhibit MMPs and may modulate cathelicidin processing) and TLR2 antagonists.
• Vitamin D / cathelicidin axis — Gombart, Borregaard, Koeffler. FASEB J 2005;19(9):1067-77. Established the CAMP gene as a direct vitamin D receptor target. This work explains the molecular basis for the well-documented seasonality of respiratory infections, the higher infection rates in vitamin D deficient populations, and the proposed protective role of vitamin D supplementation against tuberculosis and respiratory infection.
• Ocular surface — Gordon et al., 2005 (PMC1497871) and subsequent work characterized LL-37 expression in conjunctival and corneal epithelia and demonstrated potent antibacterial and antiviral activity against ocular pathogens (P. aeruginosa, S. aureus, HSV-1, adenovirus). Topical ocular formulations have been explored.
• Cancer biology (anti-cancer evidence is mixed) — LL-37 expression is altered in multiple cancers; it can be pro-tumorigenic in some contexts (breast, ovarian, lung cancer where it promotes proliferation) and anti-tumorigenic in others (gastric cancer, colon cancer where it triggers apoptosis). PMC4485164 reviews LL-37 as both potential anticancer drug and tumor-promoting factor depending on context.
• Structure-function 3D characterization — Wang G et al. Biochim Biophys Acta 2014 (PMID 24463069); Sci Rep 2020 (s41598-020-74401-5) crystal structure of tetrameric channel-forming LL-37 in detergent micelles; multiple NMR structures of LL-37 in different lipid environments. The structural biology is unusually well characterized.
• Modified analogs — Multiple synthetic LL-37 analogs have been designed to dissociate antimicrobial activity from inflammation-driving activity: D-LL-37 (D-amino acid version, more stable), KS-30, OP-145, and others. These represent the active drug-discovery pipeline for cathelicidin therapeutics.

Human Data

Human LL-37 data falls into two categories: endogenous LL-37 expression studies (correlative / observational) and small Phase 1/2 trials of exogenous LL-37 or its analogs:

• Topical synthetic LL-37 for chronic venous leg ulcers — Multiple small Phase 1/2 trials in Europe (Pep637, Promore Pharma; later Lipopeptide AB) studied topical synthetic LL-37 application to hard-to-heal venous leg ulcers. Acceptable safety; modest efficacy signals on wound-area reduction and re-epithelialization speed; no large Phase 3 confirmation.
• OP-145 ear drops for chronic suppurative otitis media — OP-145 is a synthetic LL-37-derived peptide developed for chronic ear infections. Phase 2 trials demonstrated antibacterial efficacy and acceptable safety in ear-drop formulation.
• Endogenous LL-37 levels and disease association — Large body of observational human research linking LL-37 levels to disease states: low LL-37 in atopic dermatitis (correlates with skin infection susceptibility), high LL-37 in psoriasis and rosacea (correlates with inflammation severity), low LL-37 in active tuberculosis and respiratory infection (correlates with vitamin D deficiency), reduced LL-37 in inflammatory bowel disease, altered LL-37 in periodontal disease, and many more correlations.
• Vitamin D supplementation studies — Multiple human studies have shown that oral vitamin D supplementation in deficient adults produces measurable upregulation of cathelicidin (LL-37) production from monocytes and keratinocytes — confirming the vitamin D / CAMP transcriptional axis works in vivo. Hata et al. and others demonstrated this in atopic dermatitis subjects.
• Anti-LL-37 autoantibodies in psoriasis — Small clinical studies have identified LL-37 / self-DNA complexes and anti-LL-37 antibodies in psoriasis patient sera, supporting the autoimmunity-driving role of LL-37 in that disease.
• No native-LL-37 systemic therapeutic trials — No published Phase 2/3 trial of systemic (parenteral) native LL-37 for any indication. Systemic administration faces challenges including rapid proteolytic degradation, broad pleiotropy, and dose-dependent host-cell toxicity at higher concentrations.
• Anecdotal community use — A small number of self-experimenters use synthetic LL-37 SubQ for "immune support" or "gut healing" applications. These reports lack controlled evidence and are unsupported by safety data; SubQ delivery of native LL-37 has not been characterized in any published clinical trial.

Reconstitution & Storage

Synthetic LL-37 is sold as a lyophilized powder for laboratory use. No label or pharmacopoeia sets how to mix or keep it, and what the trials used was made for them by a pharmacy: in the phase 2b leg-ulcer trial, LL-37 acetate was dissolved in sodium acetate buffer, sterile-filtered and mixed with a polyvinyl alcohol diluent just before it went on the wound (Mahlapuu et al., 2021); the diabetic-foot-ulcer cream was 0.5 mg of LL-37 per gram of base cream, and a stability test put its shelf life at 99 months at 4 °C and 75 months at 28 °C, while it melted at 40 °C (Miranda et al., 2023). Online guides describe 5 mg vials mixed with bacteriostatic water and kept in a refrigerator, used within two to three weeks.

• Salt blunts it — LL-37's killing of bacteria weakens at the salt concentration of body fluids (about 150 mM sodium chloride), which is one reason it has been hard to turn into a drug; its activity against biofilms survives high salt better (Lai & Gallo, 2009; Ridyard & Overhage, 2021).

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Side Effects & Risks

LL-37 has no approved use, and no trial has tested it injected under the skin, so what is known about its risks comes from laboratory work, from the small topical trials, and from one three-patient trial that injected it into skin tumors (ClinicalTrials.gov NCT02225366):

• Toxic to human cells at high concentrations — LL-37 is selective for microbial membranes at the concentrations that kill microbes, and the concentrations that damage human cells are generally higher (Lai & Gallo, 2009), but "high toxicity to human cells" is one of the limitations that has kept it from becoming a drug (Ridyard & Overhage, 2021).
• Inflammation amplification (autoimmunity) — In psoriatic skin, LL-37 binds self-DNA and self-RNA from dying cells and carries them into plasmacytoid dendritic cells, where TLR9 and TLR7 respond as if to an infection (Kahlenberg & Kaplan, 2013; Schauber & Gallo, 2008). Interferon-alpha follows, and with it the T-cell response that keeps psoriasis going (Reinholz et al., 2012). No trial has given LL-37 to people with psoriasis; it is what their lesional skin already overproduces (Kahlenberg & Kaplan, 2013).
• Rosacea — In rosacea, skin protease activity is raised and cathelicidin is cut into different peptide fragments than in normal skin; injecting those rosacea fragments into mouse skin produced inflammation, and mice without the cathelicidin gene did not react that way (Yamasaki et al., 2007). Whether putting LL-37 on rosacea-prone skin would do the same in people has not been tested.
• Local reactions — In the phase 2b leg-ulcer trial, two patients on the lower dose reported dermatitis and the rate of adverse events did not differ from placebo (Mahlapuu et al., 2021); in the first-in-man trial, the highest concentration, 3.2 mg/mL, brought more frequent and more severe local reactions than the lower ones (Grönberg et al., 2014, as described by Mahlapuu et al., 2021). In the ear-drop trial of the LL-37-derived peptide OP-145, no one had developed antibodies against it 8 weeks on (Peek et al., 2020).
• Bacterial resistance — Not only theoretical: Staphylococcus aureus became resistant after three passages at sub-inhibitory concentrations of LL-37 in one study and stably resistant within 168 generations in another, and Salmonella typhimurium and Clostridioides difficile did the same under prolonged exposure. Gram-positive bacteria change their surface charge through systems such as ApsTC, and Gram-negative bacteria modify their LPS; whether resistance crosses over to the antibiotic colistin is unsettled (Ridyard & Overhage, 2021).
• Cancer, direction unclear — LL-37 has been reported both to promote and to suppress tumors depending on the cancer, and reviewed as a possible anticancer drug and as a tumor-promoting factor (Wang et al., 2014; Kuroda et al., 2015; PMC4485164). The one trial that injected it into tumors treated three people with melanoma; a case report describes skin lesions appearing about 45 days into those weekly injections and clearing within two months of stopping (ClinicalTrials.gov NCT02225366; Dolkar et al., 2018).
• Pregnancy and lactation — Untested. The leg-ulcer trials excluded women who were pregnant or breastfeeding and required a negative pregnancy test (Mahlapuu et al., 2021).
• Sourcing and purity — The trials used peptide made under pharmacy or GMP conditions (Mahlapuu et al., 2021; Peek et al., 2020). LL-37 sold as a research chemical is made to no such standard, and nothing about a vial's contents is checked before sale.
• Drug interactions — Unstudied in people. In bacterial cultures LL-37 acts together with several antibiotic classes (Ridyard & Overhage, 2021); what that would mean alongside an antibiotic in a person has not been tested.

Bloodwork & Monitoring

No trial, label or guideline sets monitoring for LL-37. The trials that gave it watched for harm rather than tracking a marker: the phase 2b leg-ulcer trial recorded local tolerability and adverse events at every dressing change, vital signs weekly and blood counts and chemistry monthly, and found no consistent change in any of them (Mahlapuu et al., 2021); the ear-drop trial of the LL-37-derived peptide OP-145 added blood counts, cultures, audiometry and a test for antibodies against the peptide, which no one developed by week 8 (Peek et al., 2020). Vitamin D controls part of the body's own cathelicidin production (Gombart et al., 2005), but in the one placebo-controlled trial, 4,000 IU a day for 21 days did not significantly change cathelicidin in skin (Hata et al., 2014).

Commonly Stacked With

No published study has tested LL-37 together with another peptide in people or animals. What is published on combinations is laboratory work pairing it with antibiotics, and what the pairings below rest on is online guides.

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Legal Status

Related Compounds

Innate-immunity and tissue-repair peptides that sit next to LL-37 in the host-defense toolkit.

Next Steps

References

1. Gombart AF, Borregaard N, Koeffler HP. Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3. FASEB J. 2005;19(9):1067-1077. PMID: 15985530. (The defining vitamin D / cathelicidin transcription paper.)
2. Mookherjee N, Brown KL, Bowdish DM, Doria S, Falsafi R, Hokamp K, Roche FM, Mu R, Doho GH, Pistolic J, Powers JP, Bryan J, Brinkman FS, Hancock RE. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J Immunol. 2006;176(4):2455-2464. PMID: 16456005. (Foundational TLR-modulation paper.)
3. Mookherjee N, Hancock RE. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell Mol Life Sci. 2007;64(7-8):922-933. PMID: 17310278.
4. Wang G, Mishra B, Epand RF, Epand RM. High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments. Biochim Biophys Acta. 2014;1838(9):2160-2172. PMID: 24463069. (Structural biology review.)
5. Sancho-Vaello E, Gil-Carton D, François P, Bonetti EJ, Kreir M, Pothula KR, Kleinekathöfer U, Zeth K. The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics. Sci Rep. 2020;10(1):17356. (Crystal structure of tetrameric channel-forming LL-37.) DOI: 10.1038/s41598-020-74401-5.
6. Reinholz M, Ruzicka T, Schauber J. Cathelicidin LL-37: an antimicrobial peptide with a role in inflammatory skin disease. Ann Dermatol. 2012;24(2):126-135. PMID: 22577261.
7. Yamasaki K, Di Nardo A, Bardan A, Murakami M, Ohtake T, Coda A, Dorschner RA, Bonnart C, Descargues P, Hovnanian A, Morhenn VB, Gallo RL. Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea. Nat Med. 2007;13(8):975-980. PMID: 17676051. (Rosacea pathogenesis paper.)
8. McDermott AM. Antimicrobial compounds in tears. Exp Eye Res. 2013;117:53-61. PMID: 23880529. (Ocular surface AMP review.)
9. Gordon YJ, Huang LC, Romanowski EG, Yates KA, Proske RJ, McDermott AM. Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity. Curr Eye Res. 2005;30(5):385-394. PMID: 16020269. (PMC1497871.)
10. Schauber J, Gallo RL. The vitamin D pathway: a new target for control of the skin's immune response? Exp Dermatol. 2008;17(8):633-639. PMID: 18573153. (Vitamin D / cathelicidin in skin immunity review.)
11. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 2002;415(6870):389-395. PMID: 11807545. (Foundational AMP review.)
12. Travkova OG, Moehwald H, Brezesinski G. The interaction of antimicrobial peptides with membranes. Adv Colloid Interface Sci. 2017;247:521-532. PMID: 28606715. (Membrane disruption mechanism.)
13. Aoki W, Ueda M. Characterization of antimicrobial peptides toward the development of novel antibiotics. Pharmaceuticals (Basel). 2013;6(8):1055-1081. PMID: 24276381. (Therapeutic AMP development context.)
14. Steinhoff M, Schauber J, Leyden JJ. New insights into rosacea pathophysiology: a review of recent findings. J Am Acad Dermatol. 2013;69(6 Suppl 1):S15-S26. PMID: 24229632. (Rosacea LL-37 mechanism review.)
15. Lai Y, Gallo RL. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009;30(3):131-141. PMID: 19217824.
16. Kahlenberg JM, Kaplan MJ. Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease. J Immunol. 2013;191(10):4895-4901. PMID: 24185823. (Autoimmunity-driving role.)
17. Antimicrobial Peptides of the Cathelicidin Family: Focus on LL-37 and Its Modifications. Int J Mol Sci. 2025;26(16):8103. PMID: 40869425. (Recent comprehensive review.)
18. The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent. Antibiotics (Basel). 2021. PMC: PMC8227053. (Antibiofilm and synergy review.)
19. Innate immunity and the role of the antimicrobial peptide cathelicidin in inflammatory skin disease. PMC: PMC3904447. (Inflammatory skin disease review.)
20. Human antimicrobial/host defense peptide LL-37 may prevent the spread of a local infection through multiple mechanisms: an update. Inflamm Res. 2025. DOI: 10.1007/s00011-025-02005-8. (Most recent comprehensive update.)
21. FDA. Bulk Drug Substances Nominated for Use in Compounding Under Section 503A of the FD&C Act (503A categories list), versions updated April 15, April 22 and May 14, 2026. fda.gov/media/94155/download. Read October 3, 2026. (Notice that 12 peptides would leave Category 2 because their nominations were withdrawn; their removal; GHK-Cu, except injectable, back in Category 1.)
22. Grönberg A, Mahlapuu M, Ståhle M, Whately-Smith C, Rollman O. Treatment with LL-37 is safe and effective in enhancing healing of hard-to-heal venous leg ulcers: a randomized, placebo-controlled clinical trial. Wound Repair Regen. 2014;22(5):613-621. doi:10.1111/wrr.12211. PMID: 25041740.
23. Mahlapuu M, Sidorowicz A, Mikosinski J, Krzyżanowski M, Orleanski J, Twardowska-Saucha K, et al. Evaluation of LL-37 in healing of hard-to-heal venous leg ulcers: A multicentric prospective randomized placebo-controlled clinical trial. Wound Repair Regen. 2021;29(6):938-950. doi:10.1111/wrr.12977. PMID: 34687253.
24. Miranda E, Bramono K, Yunir E, Reksodiputro MH, Suwarsa O, Rengganis I, et al. Efficacy of LL-37 cream in enhancing healing of diabetic foot ulcer: a randomized double-blind controlled trial. Arch Dermatol Res. 2023;315(9):2623-2633. doi:10.1007/s00403-023-02657-8. PMID: 37480520.
25. Peek NFAW, Nell MJ, Brand R, Jansen-Werkhoven T, van Hoogdalem EJ, Verrijk R, et al. Ototopical drops containing a novel antibacterial synthetic peptide: Safety and efficacy in adults with chronic suppurative otitis media. PLoS One. 2020;15(4):e0231573. doi:10.1371/journal.pone.0231573. PMID: 32287316.
26. Hata TR, Kotol P, Jackson M, Nguyen M, Paik A, Udall D, et al. Administration of oral vitamin D induces cathelicidin production in atopic individuals. J Allergy Clin Immunol. 2008;122(4):829-831. doi:10.1016/j.jaci.2008.08.020. PMID: 19014773.
27. Hata TR, Audish D, Kotol P, Coda A, Kabigting F, Miller J, et al. A randomized controlled double-blind investigation of the effects of vitamin D dietary supplementation in subjects with atopic dermatitis. J Eur Acad Dermatol Venereol. 2014;28(6):781-789. doi:10.1111/jdv.12176. PMID: 23638978.
28. Dolkar T, Trinidad CM, Nelson KC, Amaria RN, Nagarajan P, Torres-Cabala CA, et al. Dermatologic toxicity from novel therapy using antimicrobial peptide LL-37 in melanoma: A detailed examination of the clinicopathologic features. J Cutan Pathol. 2018;45(7):539-544. doi:10.1111/cup.13262. PMID: 29665030.
29. Kuroda K, Okumura K, Isogai H, Isogai E. The Human Cathelicidin Antimicrobial Peptide LL-37 and Mimics are Potential Anticancer Drugs. Front Oncol. 2015;5:144. doi:10.3389/fonc.2015.00144. PMID: 26175965. PMC4485164.
30. ClinicalTrials.gov. Intratumoral Injections of LL37 for Melanoma (M.D. Anderson Cancer Center; completed). NCT02225366. Read October 4, 2026.
31. NCBI Gene. CAMP cathelicidin antimicrobial peptide [Homo sapiens], Gene ID 820 (chromosome 3p21.31, four exons). ncbi.nlm.nih.gov/gene/820. Read October 4, 2026.
32. World Anti-Doping Agency. Prohibited List 2026 (in effect January 1, 2026). S0, Non-approved substances. wada-ama.org/sites/default/files/2025-09/2026list_en_final_clean_september_2025.pdf. Read October 3, 2026.

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