LL‑37 is the active form of the human cathelicidin CAMP gene. Stored as the precursor hCAP‑18, it’s activated by proteolytic enzymes (e.g., proteinase 3). This 37‑amino‑acid, amphipathic α‑helical peptide is produced by epithelial and immune cells and is a key effector in innate immunity .
At the molecular level, LL‑37 exerts its antimicrobial action primarily through membrane disruption—forming pores that lyse pathogens. It also interacts with various host receptors (FPRL‑1, P2X7, EGFR) boosting chemotaxis, cell proliferation, angiogenesis, and immunoregulation .
Its dual role—direct pathogen killing plus signaling and tissue repair—makes it uniquely suited for treating chronic wounds and infections. LL-37, Like all Cathelicidins, has antimicrobial, antibacterial, antiviral, anti-fungal and has been shown to reduce inflammation. Research has also shows that its effect against certain cancers and encourages blood vessel growth in specific settings.
For Research Use Only
Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease

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