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IMMUNEPEPTIDE PROFILE

Cathelicidins

Also known as LL-37, CRAMP, hCAP-18, Cathelicidin antimicrobial peptides

Cathelicidins are a family of endogenous antimicrobial peptides characterized by a conserved N-terminal cathelin domain and a variable C-terminal antimicrobial peptide. LL-37 is the sole human cathelicidin — a 37-amino acid cationic peptide with broad-spectrum antimicrobial, wound-healing, and immunomodulatory activity. Research interest spans topical antimicrobials, chronic wound care, and cancer biology.

Last updated April 10, 2026

TL;DR

Quick summary

Cathelicidins are endogenous antimicrobial peptides, with LL-37 being the sole human member. LL-37 has broad-spectrum antimicrobial activity, accelerates wound healing by activating keratinocyte migration and angiogenesis, and is notably absent in chronic non-healing ulcers.

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Overview

Cathelicidins are a family of endogenous antimicrobial peptides characterized by a conserved N-terminal cathelin domain and a variable C-terminal antimicrobial peptide. LL-37 is the sole human cathelicidin — a 37-amino acid cationic peptide with broad-spectrum antimicrobial, wound-healing, and immunomodulatory activity. Research interest spans topical antimicrobials, chronic wound care, and cancer biology.

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Mechanism of action

LL-37 disrupts bacterial membranes via amphipathic alpha-helix insertion, causing membrane depolarization and lysis. It also binds lipopolysaccharide (LPS), neutralizing endotoxin. Beyond direct killing, LL-37 activates keratinocyte migration through formyl peptide receptor 2 (FPR2), triggering MAPK and PI3K/Akt signaling. It promotes angiogenesis by activating VEGFR2, and recruits neutrophils, monocytes, and T cells via FPR1. In wounds, LL-37 accelerates re-epithelialization and vascularization and is notably absent in chronic non-healing ulcers.

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Dosing protocols

PurposeRouteDosageFrequency
wound healing researchtopical50200 mcg/mLonce to twice daily

Dosing information is for educational purposes only. Consult a qualified healthcare professional before using any peptide.

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Research summary

LL-37 is found in neutrophil granules, keratinocytes, lung epithelium, and intestinal Paneth cells. Studies demonstrate that topical LL-37 accelerates healing of chronic wounds in diabetic and venous ulcer models. It shows activity against MRSA, Pseudomonas aeruginosa, and biofilms. In vitro and early-phase clinical data support its role in wound management. Paradoxically, overexpression is linked to inflammatory skin diseases (rosacea, psoriasis) and certain cancers, where LL-37 acts as a growth factor. No LL-37 drug is currently FDA-approved; clinical trials are ongoing.[1][2][3][4]

📄This section cites 4 peer-reviewed sources. View all references →
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Evidence grading

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

strong
LL-37 is sole human cathelicidinWell-established genomic and proteomic characterization of cathelicidin family
strong
Broad-spectrum antimicrobial via membrane insertionExtensive biophysical studies confirming amphipathic helix membrane disruption
preliminary
Accelerates chronic wound healingPreclinical diabetic and venous ulcer models; early-phase clinical trials only
moderate
Absent in chronic non-healing ulcersConsistent human wound fluid biomarker studies across multiple cohorts
strong
Activates keratinocyte migration via FPR2Well-characterized receptor pharmacology and signaling studies

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

§ 05

Side effects

Local irritation at application site
Pro-inflammatory at high concentrations
May exacerbate rosacea in susceptible individuals

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 Cathelicidins for synergistic effects.

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Sourcing & access

Research compound

Cathelicidins is classified as a research compound. Regulatory status varies by jurisdiction. Always verify current legal status and source from vendors providing third-party certificates of analysis (COA).

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Frequently asked questions

Cathelicidins are a family of antimicrobial peptides with a conserved cathelin domain. LL-37 is the sole human cathelicidin, a 37-amino acid cationic peptide with broad-spectrum antimicrobial, wound-healing, and immunomodulatory activity found in neutrophils, keratinocytes, and lung epithelium.

LL-37 disrupts bacterial membranes via amphipathic alpha-helix insertion, neutralizes endotoxin (LPS), activates keratinocyte migration through FPR2 receptors, promotes angiogenesis via VEGFR2, and recruits immune cells. In wounds, it accelerates re-epithelialization and vascularization.

Side effects include local irritation at application sites and pro-inflammatory effects at high concentrations. It may exacerbate rosacea in susceptible individuals. Paradoxically, LL-37 overexpression is linked to inflammatory skin diseases (rosacea, psoriasis) and certain cancers.

Topical LL-37 accelerates healing of chronic wounds in diabetic and venous ulcer models and shows activity against MRSA, Pseudomonas, and biofilms. Its absence in chronic non-healing ulcers suggests therapeutic potential, though no LL-37 drug is currently FDA-approved.

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Research references

  1. Cathelicidins: a family of endogenous antimicrobial peptidesZanetti M, et al.J Leukoc Biol, 2004PubMed
  2. LL-37 antimicrobial peptide and its roles in immunity and inflammationCederlund A, Gudmundsson GH, et al.Biochim Biophys Acta, 2011PubMed
  3. Cathelicidin LL-37 in wound healing and skin barrier functionHeilborn JD, Nilsson MF, et al.J Invest Dermatol, 2003PubMed
  4. Host defense peptides: innate immunity and therapeutic perspectivesHancock RE, Sahl HG, et al.Nat Biotechnol, 2006PubMed
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