LL-37 is a 37–amino-acid cationic antimicrobial peptide (AMP) belonging to the human cathelicidin family and encoded by the CAMP gene. It is produced as part of the innate immune system and plays a central role in host defense, immune signaling, tissue repair, and the regulation of inflammation. LL-37 is the only known cathelicidin in humans, making it a uniquely important molecule in epithelial and immune protection.
LL-37 is generated from its precursor hCAP18, a pro-peptide stored in neutrophil granules and produced by various epithelial and immune cells. During infection or tissue injury, hCAP18 is cleaved to release the active LL-37 fragment, which rapidly interacts with pathogens, host cell membranes, and immune receptors, exhibiting a wide spectrum of biological activities.
LL-37 adopts a long, flexible amphipathic α-helical structure in membrane-like environments. This arrangement presents hydrophobic residues on one face and positively charged residues on the other, allowing the peptide to:
These properties underpin LL-37’s broad-spectrum antimicrobial capabilities.
LL-37 carries a strong net positive charge, which promotes electrostatic attraction to negatively charged components of microbial surfaces such as lipopolysaccharide (LPS) in Gram-negative bacteria and teichoic acids
in Gram-positive organisms. Mammalian cell membranes are comparatively less anionic, which contributes to LL-37’s preferential binding to microbial targets.
In addition to its direct antimicrobial actions, LL-37 functions as an immunomodulatory peptide through interactions with multiple host receptors, including:
Through these pathways, LL-37 acts as a bridge between innate immunity, inflammation control, and tissue healing.
LL-37 has been shown to exhibit activity against a wide array of microorganisms, including:
Mechanisms include membrane disruption, interference with intracellular targets, and binding/neutralization of bacterial endotoxins such as LPS, which can blunt excessive inflammatory responses.
LL-37 is also recognized as a powerful immunomodulator. In experimental systems it can:
These activities help maintain a balanced immune response, supporting pathogen clearance while limiting collateral tissue damage.
LL-37 contributes to tissue repair processes across skin and mucosal surfaces. Research indicates that it:
Taken together, these effects position LL-37 as a key peptide in models of wound healing and regenerative biology.
LL-37 is expressed at various mucosal surfaces, including the gastrointestinal tract, where it:
These properties make LL-37 an important tool in research on inflammatory bowel conditions, epithelial permeability, and mucosal immunity.
In controlled experimental settings, LL-37 is commonly used to explore:
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