What is LL-37?
LL-37 is the only cathelicidin antimicrobial peptide produced by the human body. It is a 37-amino-acid peptide that serves as one of the innate immune system’s primary defenses against bacteria, viruses, fungi, and certain parasites. Its name reflects its structure: it begins with two leucine amino acids, represented by “LL,” and contains 37 amino acids.
The body produces LL-37 from a precursor protein called hCAP-18, or human cationic antimicrobial protein 18 kDa. When the immune system detects a threat, enzymes cleave hCAP-18 and release active LL-37. This occurs in neutrophils, macrophages, dendritic cells, natural killer cells, and epithelial cells throughout the body, particularly in the skin, lungs, and gastrointestinal tract.
LL-37 is unusually versatile. It can disrupt microbial membranes, modulate immune signaling, neutralize bacterial toxins, support wound repair, and stimulate angiogenesis. Because it acts through multiple pathways at once, pathogens may have more difficulty developing resistance to it than they do to many conventional antibiotics.
LL-37 has gained significant attention as antimicrobial resistance becomes a growing global health concern. Rather than acting only as a direct antimicrobial agent, it works as part of the body’s own immune-defense network. Clinical research has also tested topical LL-37 in wound-healing settings, including venous leg ulcers and diabetic foot ulcers.