Human cathelicidin antimicrobial peptide
LL-37
Cationic host-defence peptide that disrupts microbial membranes and modulates innate immune signalling.
Primary Mechanism of Action
Clinical / Scientific
LL-37 is the C-terminal peptide of human cathelicidin (hCAP18). It forms pores in microbial membranes and also acts as an alarmin, modulating TLR signalling, chemotaxis, and epithelial repair. Therapeutic use of exogenous LL-37 remains experimental because host cytotoxicity and are dose-dependent.
Pathway Targets
Microbial membranes
Scientific explanation
Cationic pore-forming activity.
Innate immune signalling
Scientific explanation
Alarmin / immunomodulatory effects.
Pathway Convergence
Clinical / Scientific
Target → pathway → downstream effect → biological consequence. This is a mechanistic map, not a treatment claim.
Receptor to physiology
Target to downstream effect: Microbial membranes → Innate immune signalling
Mechanistically Relevant Repurposed & Adjunctive Applications
Research peptide context
PreclinicalMechanistic rationale
Catalogued as a research peptide. Mechanistic statements below describe known or pathway biology and do not establish a licensed therapeutic indication.
Mechanistic Application Matrix
| Biological Target | Mechanism | Potential Relevance | Evidence Level |
|---|---|---|---|
| Microbial membranes | Pore formation | Host defence | Established mechanism |
| TLR / chemokine signalling | Immunomodulation | Innate immunity | Established mechanism (endogenous peptide) |
In Plain Language
LL-37 is one of the body’s own antibiotic peptides: it punches holes in many microbes and also waves a flag to the immune system. Using extra LL-37 as a drug is still experimental.
Mechanistic information is provided for scientific and educational purposes. Discussion of biological pathways or investigational applications does not establish clinical efficacy or constitute individualized medical advice.