Research Compound LL-37 is a laboratory material for analytical and in vitro work.
What is LL-37?
LL-37 is a 37-amino-acid peptide beginning with two leucines (hence the name), with a molecular weight of approximately 4.5 kDa. It is the only human cathelicidin, produced by cleavage of the C-terminal part of the precursor protein hCAP18, primarily by proteinase 3.
Research background
Human cathelicidin was described in the mid-1990s, a period when antimicrobial peptides were recognised as an important part of mammalian innate immunity. LL-37 has since become one of the most studied human antimicrobial peptides.
Mechanism and scientific context
In solution LL-37 forms a positively charged amphipathic alpha-helix, allowing it to interact with and disrupt negatively charged bacterial membranes. Beyond direct antimicrobial activity in vitro, it is studied as an immunomodulator: it binds lipopolysaccharide, influences chemotaxis and activates receptors such as FPR2.
Main research areas
- antimicrobial peptides and membrane interactions
- innate immunity
- immunomodulation and chemotaxis
- bacterial antibiotic resistance
Level of evidence
Strong mechanistic and preclinical literature. There is no basis for independent therapeutic use of the research material.
Research use only: for laboratory, analytical and in vitro research only; not for use in humans or animals. Guidance on batch documentation is available in our COA guide.