LL-37
Human cathelicidin antimicrobial peptide — the body's primary endogenous antibiotic, with wound healing and immune defense roles
LL-37 is the only cathelicidin antimicrobial peptide expressed in humans, derived from the cleavage of the precursor protein hCAP18. It is found in neutrophils, keratinocytes, epithelial cells, and plasma, and serves as a critical first-line defense against bacterial, viral, and fungal pathogens. Its name reflects its 37-amino acid length and leucine-leucine N-terminal residues.
Beyond direct antimicrobial activity — disrupting microbial membranes and combating biofilms — LL-37 acts as an immune modulator, recruiting immune cells to infection sites, stimulating angiogenesis, and promoting wound closure. Deficiency in LL-37 is associated with recurrent skin infections in atopic dermatitis and poor wound healing in chronic wounds.
Exogenous LL-37 is being explored clinically for chronic wound management, antibiotic-resistant infections, and as a potential adjunct in cancer immunotherapy. Its broad-spectrum antimicrobial properties and tolerability make it a unique peptide at the intersection of innate immunity and tissue repair.
Primary Benefits
Synthetic peptide derived from human gastric juice, known for accelerating tissue repair and reducing inflammation
Immunomodulating peptide studied across immune dysfunction, chronic infections, and oncology support — approved in 35+ countries
Alpha-MSH derived tripeptide with potent anti-inflammatory and gut healing properties, oral or subcutaneous