LL-37 Human Cathelicidin Research Hub
LL-37 cathelicidin research — human antimicrobial peptide mechanisms, immunomodulation, wound healing, anti-biofilm activity, innate immunity, and infection defense studies with PubMed citations.
Featured Research
In-depth research profiles with mechanisms of action, key findings, and peer-reviewed citations.
LL-37 (Cathelicidin)
Also known as: LL-37, Cathelicidin, CAP18, hCAP18
LL-37 is the only human cathelicidin antimicrobial peptide, derived from the C-terminal cleavage of the 18-kDa precursor protein hCAP18 by proteinase 3. It is a 37-amino-acid amphipathic alpha-helical peptide produced by neutrophils, macrophages, epithelial cells, and other cell types as part of the innate immune defense. LL-37's antimicrobial mechanism involves direct membrane disruption of micr...
Quick Facts
Sequence: Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-...
MW: 4493.33 g/mol
CAS: 154947-66-7
Store lyophilized powder at -20C. LL-37 is susceptible to proteolytic degradation; reconstitute in sterile water and sto...
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Read ArticleResearch Applications
Key research categories and applications studied in the scientific literature.
Immune Support
Acts as a crucial part of the innate immune system, functioning as a natural antibiotic to directly neutralize microbes and activate dendritic cells to detect threats.
Recovery & Healing
Beyond antimicrobial activity, LL-37 promotes wound closure through angiogenesis and re-epithelialization, and inhibits biofilm formation at wound sites.
Anti-Biofilm Research
LL-37 disrupts established bacterial biofilms — a major challenge in chronic wound and medical device infection research.
Frequently Asked Questions
Common questions about ll-37 research research, purity standards, and sourcing.
What is LL-37?
LL-37 is the only cathelicidin-derived antimicrobial peptide in humans. It is a 37-amino acid peptide cleaved from the precursor protein hCAP18 and plays critical roles in innate immunity, directly killing bacteria, fungi, and some viruses through membrane disruption.
How does LL-37 fight infection?
LL-37 disrupts microbial membranes through electrostatic interaction with negatively charged lipid bilayers. Beyond direct antimicrobial activity, it modulates immune cell recruitment, inhibits biofilm formation, and promotes wound closure through angiogenesis and re-epithelialization.
What makes LL-37 unique among antimicrobial peptides?
LL-37 is the sole human cathelicidin — unlike defensins which have multiple family members. Its dual role as both a direct antimicrobial agent and an immune modulator makes it a central player in the innate immune response and a promising research target.
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