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Research Monograph

LL-37 (Human Cathelicidin Antimicrobial Peptide)

Also Known AshCAP-18 · CAMP · Human Cathelicidin · FALL-39 · Cathelicidin antimicrobial peptide

Molecular Weight4493.33 g/mol
Discovered1995
Citations5 peer-reviewed
Research Areas5 domains
Background

The only human cathelicidin antimicrobial peptide, derived by proteolytic cleavage of the 18 kDa precursor protein hCAP-18 by proteinase 3 in neutrophil granules. Named for its N-terminal Leu-Leu dipeptide and 37-residue length. Expressed in neutrophils, epithelial cells, macrophages, and other cell types. First characterized in the mid-1990s.

Amino Acid SequenceLeu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser
Mechanisms of Action

How LL-37 Works

01

Membrane Disruption (Direct Antimicrobial)

LL-37 adopts an amphipathic alpha-helical conformation in membrane environments. The cationic face interacts electrostatically with negatively charged bacterial membranes (LPS in Gram-negatives, lipoteichoic acid in Gram-positives), while the hydrophobic face inserts into the lipid bilayer. This creates transmembrane pores or carpet-like disruption, leading to osmotic lysis. Selectivity for bacterial over mammalian membranes is driven by the charge difference (bacterial membranes are more anionic).

bacterial membrane phospholipidsLPSlipoteichoic acid
02

Chemotactic & Immunomodulatory Signaling

LL-37 activates formyl peptide receptor-like 1 (FPRL1/FPR2), a G-protein-coupled receptor on neutrophils, monocytes, and T-cells, driving chemotaxis of immune cells to infection sites. It also modulates TLR signaling — LL-37 binds extracellular DNA and RNA, facilitating endosomal TLR9 and TLR7/8 activation while dampening surface TLR4 signaling from LPS.

FPRL1/FPR2TLR9TLR7/8TLR4neutrophilsmonocytes
03

Anti-Biofilm Activity

LL-37 disrupts bacterial biofilms at sub-inhibitory concentrations by reducing initial bacterial attachment, stimulating twitching motility (in Pseudomonas aeruginosa), and interfering with quorum sensing signaling. This anti-biofilm activity is mechanistically distinct from its direct antimicrobial action and occurs at concentrations below those needed for planktonic killing.

biofilm matrixbacterial attachmentquorum sensingtwitching motility
04

Wound Healing & Angiogenesis

LL-37 promotes wound healing through EGFR transactivation (via metalloprotease-mediated HB-EGF shedding) and direct VEGF-mediated angiogenesis via FPRL1. It stimulates epithelial cell migration and proliferation in wound models and promotes neovascularization at wound sites.

EGFRHB-EGFVEGFFPRL1epithelial migration
Evidence-Graded Research Areas

Published Research

Strong
Moderate
Emerging
Preclinical

Antimicrobial Defense

Strong

LL-37 shows broad-spectrum activity against Gram-positive and Gram-negative bacteria, fungi (Candida spp.), and enveloped viruses. MIC values typically range from 1-32 micromolar depending on organism and assay conditions. Importantly, bacterial resistance development to LL-37 is rare compared to conventional antibiotics, as the membrane-targeting mechanism requires fundamental changes in membrane composition.

Biofilm Infections

Moderate

Clinically, biofilms cause >60% of chronic infections. LL-37 shows unique anti-biofilm activity at sub-MIC concentrations against P. aeruginosa, S. aureus, and other biofilm-forming pathogens. Mechanisms include prevention of initial attachment, disruption of established matrix, and interference with quorum sensing. Clinical relevance for chronic wound, implant, and pulmonary infections.

Innate Immune Regulation

Moderate

LL-37 bridges innate and adaptive immunity through chemokine-like activity (FPRL1-mediated immune cell recruitment), modulation of dendritic cell differentiation, and regulation of TLR signaling. Deficiency states (morbus Kostmann, specific granule deficiency) are associated with increased infection susceptibility, validating its non-redundant immune role.

Wound Repair

Moderate

LL-37 is upregulated in wound fluid and at wound margins. It promotes re-epithelialization through EGFR transactivation and angiogenesis through FPRL1-VEGF signaling. In diabetic wound models (where endogenous LL-37 expression is impaired), exogenous LL-37 application restores healing trajectory.

Autoimmunity (Psoriasis, Rosacea)

Strong

LL-37 is overexpressed in psoriatic lesions where it forms complexes with self-DNA, activating plasmacytoid dendritic cells via TLR9 and driving IFN-alpha production — a key pathogenic step in psoriasis. In rosacea, aberrant cathelicidin processing produces inflammatory peptide fragments. This dual role — protective in infection, pathogenic in autoimmunity — illustrates the complexity of host defense peptide biology.

Safety Profile

LL-37 is an endogenous human peptide expressed constitutively and inductively at epithelial surfaces. At physiological concentrations, it is selective for microbial membranes over host cell membranes. At supraphysiological concentrations (>25 micromolar), cytotoxicity to mammalian cells can occur due to loss of membrane selectivity. Topical and local administration routes minimize systemic exposure. The role in autoimmune pathology (psoriasis, rosacea) reflects dysregulated expression rather than inherent toxicity. No human clinical trial data for exogenous LL-37 administration is available from completed studies.

Handling & Storage

LL-37 is a 37-residue amphipathic peptide that readily adsorbs to plastic and glass surfaces. Use low-binding microcentrifuge tubes and pipette tips. Reconstitute with sterile water or bacteriostatic water. Store lyophilized at -20°C. Reconstituted solutions at 2-8°C, use within 14 days. The peptide can aggregate at high concentrations — keep working solutions dilute.

References & Citations

Peer-Reviewed Literature

  1. 1

    A comprehensive summary of LL-37, the factotum human cathelicidin peptide

    Vandamme D, Lanber B, Vergote I, Bhatt T.

    Cellular Immunology, 2012PubMed 22999507DOI
  2. 2

    Human host defense peptide LL-37 prevents bacterial biofilm formation

    Overhage J, Campisano A, Bains M, et al.

    Infection and Immunity, 2008PubMed 18347040DOI
  3. 3

    Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide

    Lande R, Gregorio J, Facchinetti V, et al.

    Nature, 2007PubMed 17943085DOI
  4. 4

    The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium

    Heilborn JD, Nilsson MF, Kratz G, et al.

    Journal of Investigative Dermatology, 2003PubMed 12648222DOI
  5. 5

    An angiogenic role for the human peptide antibiotic LL-37/hCAP-18

    Koczulla R, von Degenfeld G, Kupatt C, et al.

    Journal of Clinical Investigation, 2003PubMed 12618519DOI
Frequently Asked Questions

LL-37 FAQ

What is LL-37?

LL-37 is the only human cathelicidin antimicrobial peptide — a 37-amino-acid, amphipathic, alpha-helical peptide produced by neutrophils, epithelial cells, and macrophages. It has broad-spectrum antimicrobial activity, anti-biofilm properties, and immunomodulatory functions that bridge innate and adaptive immunity.

How does LL-37 kill bacteria?

LL-37 adopts an alpha-helical structure that inserts into negatively charged bacterial membranes, forming pores or carpet-like disruptions that cause osmotic lysis. Selectivity for bacterial over mammalian membranes is driven by the greater negative charge density of bacterial membrane phospholipids compared to the neutral (zwitterionic) mammalian cell surface.

Why is LL-37 relevant to biofilm infections?

LL-37 disrupts biofilms at concentrations below those needed to kill planktonic bacteria. It prevents initial bacterial attachment, stimulates bacterial motility (reducing sessile growth), and interferes with quorum sensing. This is clinically relevant because biofilms cause >60% of chronic infections and are resistant to conventional antibiotics.

Is LL-37 involved in autoimmune conditions?

Yes. In psoriasis, overexpressed LL-37 binds self-DNA released from damaged keratinocytes, forming complexes that activate plasmacytoid dendritic cells via TLR9, triggering IFN-alpha production and driving the inflammatory cascade. This illustrates that host defense peptides can be pathogenic when dysregulated.

How should LL-37 be handled?

LL-37 adsorbs readily to standard plastic and glass surfaces — use low-binding tubes and tips. Store lyophilized at -20°C. Reconstitute with sterile or bacteriostatic water; keep reconstituted solution at 2-8°C and use within 14 days. Avoid high concentration stocks as LL-37 can self-aggregate.

Available for Research

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All compounds 99%+ purity, verified by Janoshik Analytical. GMP-manufactured lyophilized powder.

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Disclaimer: This monograph is provided for educational and research purposes only. G26x Peptides products are sold exclusively as research chemicals. They are not intended for human consumption, therapeutic use, or as dietary supplements. All research should be conducted in compliance with applicable laws and institutional review board protocols. Information presented here is sourced from published peer-reviewed literature and does not constitute medical advice.