LL-37 Research Hub — Cathelicidin Antimicrobial Peptide Studies
LL-37 is the only human cathelicidin-derived antimicrobial peptide, a 37-residue amphipathic α-helical peptide widely studied in innate-immunity, antimicrobial and tissue-repair research literature.
What this hub covers
- Cathelicidin / CAMP gene biology
- Membrane-disruptive antimicrobial mechanism
- Immunomodulatory signalling (FPR2, P2X7)
- Tissue-repair and wound-research literature
LL-37 research articles
All research →LL-37 Research Overview
LL-37 is the only human cathelicidin — a 37-residue cationic amphipathic alpha-helical host defence peptide derived from the CAMP gene product hCAP-18, studied for its broad-spectrum direct antimicrobial activity, immunomodulation of innate and adaptive immunity, wound healing promotion, anti-biofilm properties, angiogenesis induction, and complex roles in cancer biology.
Read article →Related research hubs
Researchers studying LL-37 commonly cross-reference these compounds.
BPC-157 is a stable pentadecapeptide fragment derived from human gastric juice protein. It is one of the most extensively cited compounds in tissue-repair and angiogenesis research, frequently studied alongside Thymosin Beta-4 (TB-500).
Explore hub →TB-500 is a synthetic peptide corresponding to the active region of naturally occurring Thymosin Beta-4 — one of the most abundant actin-sequestering proteins in mammalian cells. It is widely studied in tissue-repair, angiogenesis and cell-migration research.
Explore hub →LL-37 research FAQ
- What is LL-37?
- LL-37 is the 37-amino-acid C-terminal active fragment of the human cathelicidin antimicrobial peptide precursor hCAP-18, widely cited in innate-immunity and antimicrobial research.
All content on this hub is provided strictly for laboratory research purposes. Compounds listed are not for human or veterinary consumption. See our research-use disclosure for full terms.