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IMMUNEPEPTIDE PROFILE

LL-37

Also known as Cathelicidin, hCAP-18 fragment

LL-37 is the only human cathelicidin antimicrobial peptide, a 37-amino-acid peptide cleaved from the precursor protein hCAP-18. It is produced by immune cells (neutrophils, macrophages), epithelial cells, and keratinocytes as part of the innate immune response. It has broad-spectrum antimicrobial activity against bacteria, viruses, and fungi, and plays a role in wound healing and immune modulation.

Last updated April 10, 2026

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LL-37: quick citable summary

LL-37 is listed by PeptaHub as a immune peptide with a reclassification pending legal-status classification. The page summarizes mechanism, research context, common routes, safety notes, and references for writers and AI answer engines.

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PeptaHub. “LL-37: Mechanism, Research Context, Safety.” peptahub.com, 2026. https://peptahub.com/peptides/ll-37. Licensed CC BY 4.0.

License: Creative Commons Attribution 4.0 International. Link back to https://peptahub.com/peptides/ll-37.

SAMEAS / EXTERNAL IDS
LL-37 CAS: 154947-66-7
QUICK ANSWER

What is LL-37?

LL-37 is the only human cathelicidin antimicrobial peptide, a 37-amino acid fragment of hCAP-18 with broad-spectrum activity against bacteria, viruses, and fungi. Its human evidence is a single 34-patient trial of topical LL-37 on venous leg ulcers; injected use is untested.

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Overview

LL-37 is the only human cathelicidin antimicrobial peptide, a 37-amino-acid peptide cleaved from the precursor protein hCAP-18. It is produced by immune cells (neutrophils, macrophages), epithelial cells, and keratinocytes as part of the innate immune response. It has broad-spectrum antimicrobial activity against bacteria, viruses, and fungi, and plays a role in wound healing and immune modulation.

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Mechanism of action

LL-37 has a helical amphipathic structure that allows it to insert into and disrupt microbial cell membranes, creating pores and causing lysis. Beyond direct antimicrobial action, it modulates the immune response by recruiting immune cells (chemotaxis), promoting wound healing, inhibiting biofilm formation, neutralizing bacterial endotoxins (LPS), and modulating TLR signaling. Vitamin D regulates LL-37 expression, linking vitamin D deficiency to increased infection susceptibility.

§ 03

Reported study ranges

PurposeRouteReported rangeFrequency
immune supportsubcutaneous50100 mcgdaily

Reported ranges are for research context only. Consult a qualified healthcare professional before using any peptide.

Convert LL-37 research-range units

Need to convert mg to mcg, dose volume, or U-100 syringe units? The LL-37 dose calculator is preloaded with these ranges, or use the general dose unit converter.

§ 04

Research summary

Extensive research on innate immunity. Studies show broad-spectrum activity against MRSA, E. coli, Pseudomonas, Candida, and enveloped viruses including influenza and HIV. Anti-biofilm activity demonstrated against surgical implant infections. One first-in-man randomized placebo-controlled trial in 34 patients with hard-to-heal venous leg ulcers found topical LL-37 at 0.5 and 1.6 mg/mL improved healing-rate constants versus placebo and was well tolerated, with no benefit at the highest 3.2 mg/mL dose (Grönberg, Wound Repair Regen 2014). That is the only controlled human efficacy trial. Vitamin D upregulates cathelicidin gene expression, which is the proposed mechanistic link between vitamin D status and innate immune defence.[1][2][3][4][5][6]

📄This section cites 6 peer-reviewed sources. View all references →
§ 04b

Evidence grading

Each claimed benefit is graded by the strength of available evidence. Grades reflect study quality, not effect size.

moderate
Broad-spectrum antimicrobial activityDurr Biochim Biophys Acta 2006 + Bucki 2010 review; extensive in vitro and animal data vs MRSA, Pseudomonas, Candida
preliminary
Chronic wound healing promotionGrönberg Wound Repair Regen 2014: one first-in-man randomized placebo-controlled trial, n=34 venous leg ulcers, topical LL-37. Improved healing predictors at 0.5 and 1.6 mg/mL, no benefit at 3.2 mg/mL. Single small trial, surrogate endpoints, no replication
moderate
Vitamin D-mediated immune functionBucki Arch Immunol Ther Exp 2010 review: the cathelicidin gene carries a vitamin D response element and vitamin D upregulates LL-37 expression. The mechanism is well established; whether raising LL-37 by supplementation reduces infection is not
preliminary
Anti-biofilm activityIn vitro studies on surgical implant biofilm models; no completed human biofilm eradication trials
preliminary
Macrophage phagocytosis enhancementWan et al. J Leukoc Biol 2014: in vitro human macrophage assays; mechanism confirmed, translation untested

Strong = multiple RCTs · Moderate = limited trials or observational · Preliminary = animal or in vitro only · Insufficient = anecdotal or no published data

§ 05

Side effects

Injection site reactions
Redness/swelling
Mild fever (rare, immune activation)

Side effects vary by individual. This is not an exhaustive list. Report unusual symptoms to a healthcare professional.

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Common stacks

Peptides commonly paired with LL-37 for synergistic effects.

§ 08

Sourcing & access

Reclassification in progress

LL-37is one of 12 peptides the FDA removed from its Category 2 “do not compound” list on April 15, 2026, after the original nominations were withdrawn. That removal did not place it on the 503A Bulks List or into Category 1, so it is not currently eligible for compounding. The Pharmacy Compounding Advisory Committee is reviewing these substances for the Bulks List; adding one requires formal rulemaking, which typically takes 12 to 24 months. See our regulatory status tracker and regulatory timeline for the current position.

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Frequently asked questions

LL-37 is a 37-amino acid antimicrobial peptide cleaved from the precursor protein hCAP-18. It is produced by immune cells and epithelial cells as part of the innate immune response and has broad-spectrum activity against bacteria (including MRSA), viruses, and fungi.

LL-37 has an amphipathic helical structure that inserts into and disrupts microbial cell membranes. Beyond direct antimicrobial action, it recruits immune cells, promotes wound healing through angiogenesis, inhibits biofilm formation, and neutralizes bacterial endotoxins.

Reported side effects include injection site reactions, redness or swelling, and rare mild fever attributed to immune activation. LL-37 is not FDA-approved and is available only as a research peptide. The human safety data come from a single 34-patient topical wound-healing trial, in which no local or systemic safety concerns were reported. Long-term and systemic safety in humans is not characterized.

Vitamin D regulates LL-37 gene expression through the vitamin D receptor, which binds a response element in the cathelicidin gene. This pathway is the proposed mechanism linking vitamin D deficiency to greater susceptibility to infection. Whether raising LL-37 through supplementation reduces infections in practice has not been settled by trials.

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Research references

  1. LL-37, the only human member of the cathelicidin family of antimicrobial peptidesDürr UHN, Sudheendra US, Ramamoorthy ABiochim Biophys Acta, 2006PubMed
  2. Cathelicidin LL-37: a multitask antimicrobial peptideBucki R, Leszczyńska K, Namiot A, et al.Arch Immunol Ther Exp (Warsz), 2010Review
  3. Therapeutic Potential of Cathelicidin Peptide LL-37, an Antimicrobial Agent, in a Murine Sepsis ModelNagaoka I, Tamura H, Reich JInt J Mol Sci, 2020PubMed
  4. The Human Cathelicidin Antimicrobial Peptide LL-37 and Mimics are Potential Anticancer DrugsKuroda K, Okumura K, Isogai H, et al.Front Oncol, 2015PubMed
  5. Antimicrobial peptide LL-37 promotes bacterial phagocytosis by human macrophagesWan M, van der Does AM, Tang X, Lindbom L, et al.J Leukoc Biol, 2014PubMed
  6. Treatment with LL-37 is safe and effective in enhancing healing of hard-to-heal venous leg ulcers: a randomized, placebo-controlled clinical trialGrönberg A, Mahlapuu M, Ståhle M, Whately-Smith C, Rollman OWound Repair Regen, 2014PubMed
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