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LL-37
Also known as: Cathelicidin, hCAP-18
A human antimicrobial peptide of the cathelicidin family, studied for its broad-spectrum antimicrobial and immunomodulatory properties.
Quick Facts
- Sequence
- LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
- Molecular Weight
- 4493.37 Da
Overview
LL-37 is the only cathelicidin-derived antimicrobial peptide found in humans. It is a 37-amino acid peptide cleaved from the C-terminus of the human cathelicidin antimicrobial protein hCAP-18. It is expressed by various cell types including neutrophils, epithelial cells, and macrophages.
Research interest in LL-37 spans antimicrobial applications, wound healing, immune modulation, and potential anti-cancer properties.
Mechanism of Action
LL-37 disrupts microbial membranes through electrostatic interactions with negatively charged phospholipids. Beyond direct antimicrobial action, it acts as an immune modulator by binding to formyl peptide receptor-like 1 (FPRL1), promoting angiogenesis, and modulating inflammatory cytokine production. It also has chemotactic properties for various immune cells.
Biological Pathways
Research Findings
In vitro studies demonstrate broad-spectrum activity against bacteria, fungi, and enveloped viruses. Animal models show efficacy in wound healing and infection control. Early-phase human trials have explored topical applications for chronic wounds and venous leg ulcers. Some studies suggest anti-biofilm properties. Cancer research shows both pro- and anti-tumor effects depending on context.
Risks & Safety Concerns
At high concentrations, LL-37 can be cytotoxic to host cells. Potential for pro-inflammatory effects in certain contexts. May promote tumor growth in some cancer types. Systemic administration carries risk of hemolysis and toxicity. Stability and delivery remain challenges for therapeutic development.
Regulatory & Legal Status
LL-37 is available as a research peptide. It is not approved as a therapeutic by the FDA. Several clinical trials are ongoing or completed for specific applications.
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