LL-37
Human cathelicidin antimicrobial peptide (hCAP-18 active form)
The body's antimicrobial peptide.
Half-life
~ short (protease-sensitive in vivo)
Mol. weight
4493.3 g/mol
Sequence
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
Discussions
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Overview
The active C-terminal fragment of human cathelicidin (hCAP-18), an antimicrobial peptide that directly kills bacteria, fungi, and viruses by disrupting their membranes and simultaneously modulates immune and inflammatory responses. It is a key effector of innate immunity — the body's chemical first line of defense that acts before adaptive antibodies form.
Mechanism of action
LL-37 is a cationic amphipathic peptide that physically disrupts microbial membranes through electrostatic binding and pore formation, killing bacteria, fungi, and enveloped viruses directly. Beyond direct killing, it acts as an immune modulator: it recruits immune cells (chemotaxis), regulates inflammatory signaling, and promotes wound healing and angiogenesis. This dual role — direct antimicrobial plus immunomodulatory — is characteristic of the cathelicidin family and is why LL-37 is studied well beyond simple infection control.
Researched benefits
- Direct broad-spectrum antimicrobial activity
- Immune modulation and immune-cell recruitment
- Studied for wound healing and tissue repair
Considerations
- Research stage for exogenous use
- Can have pro-inflammatory effects in some contexts
- Professional guidance advised
Key Academic Literature & Studies
Search more in PubMedPeer-reviewed citations and clinical trials evaluating LL-37 in scientific literature.
Query PubMed for recent peer-reviewed preclinical and clinical publications on LL-37:
View LL-37 index on PubMed (NCBI)