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Experimental

LL-37

Human Cathelicidin Antimicrobial Peptide

LL-37 is the only cathelicidin-derived antimicrobial peptide found in humans. It is produced by immune cells, epithelial cells, and other tissues as a first-line defense against pathogens. Beyond direct antimicrobial activity, published research documents LL-37's roles in immune cell recruitment, inflammation modulation, wound healing, and biofilm disruption. It sits at the intersection of antimicrobial defense and tissue repair — two processes the body rarely separates.

Aliases: Cathelicidin, Human antimicrobial peptide

Research score
6/10
Reality tier
emerging

Mechanism

LL-37 is the sole human cathelicidin antimicrobial peptide, a 37-amino acid alpha-helical peptide derived from proteolytic cleavage of the 18kDa precursor hCAP-18. It operates through multiple mechanisms: direct antimicrobial action via membrane disruption (oligomerizes to form transmembrane pores in bacterial membranes), LPS/endotoxin neutralization, chemotaxis of immune cells (neutrophils, monocytes, T-cells), inhibition of neutrophil apoptosis, stimulation of angiogenesis and tissue regeneration, and modulation of cytokine release (IL-8, TNF-alpha). Its production is upregulated by vitamin D3, bacterial products, and inflammation.

Evidence note

Experimental — Well-characterized as a natural immune peptide with extensive in-vitro and animal data. Clinical research ongoing for wound healing and infection. No completed human RCTs for injectable use. The mechanism is well-established but therapeutic application is early-stage.

Reference data

Molecular formula
C205H340N60O53
Sequence
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES

Studies

  • LL-37, the only human member of the cathelicidin family

    Comprehensive review of LL-37's antimicrobial, immunomodulatory, and wound healing properties.

    Open source · PMID 16352721

  • Cathelicidin antimicrobial peptide in wound healing

    LL-37 promotes wound vascularization and re-epithelialization.

    Open source · PMID 18036595

  • Cathelicidin LL-37: a multitask antimicrobial peptide

    LL-37 is antimicrobial, chemoattractant, anti-apoptotic, and angiogenic; production is regulated by vitamin D3.

    Open source · PMID 20049649

FAQ

How does LL-37 disrupt biofilms?

LL-37 interferes with bacterial quorum sensing (communication) and destabilizes the extracellular matrix that protects biofilm communities. Published research shows LL-37 can penetrate and disrupt established biofilms at concentrations where conventional antibiotics fail.

How is it different from other immune peptides?

LL-37 has direct antimicrobial activity (kills bacteria) in addition to immune signaling, unlike purely signaling peptides like Thymosin Alpha-1.

What is LL-37?

The only cathelicidin antimicrobial peptide produced by the human body. It serves as part of the innate immune defense system.

For research and educational use only. This content is not medical advice.