LL-37
The sole human cathelicidin — a 37-amino-acid cationic peptide derived from the precursor hCAP18 — that disrupts microbial membranes, neutralizes inflammatory signals, and bridges innate immunity with tissue repair.
The sole human cathelicidin — a 37-amino-acid cationic peptide derived from the precursor hCAP18 — that disrupts microbial membranes, neutralizes inflammatory signals, and bridges innate immunity with tissue repair.
LL-37 disrupts bacterial membranes through electrostatic interaction with anionic lipopolysaccharide, forming transmembrane pores that lead to microbial lysis. It binds and neutralizes LPS to attenuate septic inflammatory signaling, activates TLR4 and P2X7R to prime macrophage responses, and promotes keratinocyte and endothelial cell migration via EGFR and FPRL1 signaling to accelerate wound closure. It also modulates neutrophil apoptosis to calibrate inflammatory resolution.
- [1]Vandamme D, et al. (2012). A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cellular Immunology, 280(1):22-35.
- [2]Nijnik A, Hancock RE. (2009). Host defence peptides: antimicrobial and immunomodulatory activity and potential applications for tackling antibiotic-resistant infections. Emerging Health Threats Journal, 2:e1.
- [3]Koczulla R, et al. (2003). An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. Journal of Clinical Investigation, 111(11):1665-1672.
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