LL37

LL-37 is a cationic, amphipathic peptide consisting of 37 amino acids. It represents the active C-terminal fragment of the human cathelicidin antimicrobial protein (hCAP18). As a critical component of the innate immune system, LL-37 is expressed in various cells, including neutrophils, macrophages, and epithelial cells. In research settings, LL-37 is extensively studied for its broad-spectrum…

Description

Research & Mechanisms

1. Biofilm Disruption A significant area of research for LL-37 is its potential to inhibit and degrade bacterial biofilms. Unlike traditional antibiotics, LL-37 targets the integrity of the bacterial cell membrane. Preclinical studies have shown it can penetrate and disrupt established biofilms of pathogens like Pseudomonas aeruginosa and Staphylococcus aureus, making it a key compound in antimicrobial resistance research.

2. Immune Modulation and Chemotaxis LL-37 acts as a chemoattractant, signaling immune cells (such as mast cells and leukocytes) to move toward sites of infection or injury. Researchers investigate this mechanism to understand how the peptide links the innate and adaptive immune systems, promoting the clearance of pathogens while neutralizing pro-inflammatory endotoxins (LPS).

3. Wound Healing and Angiogenesis Experimental models suggest that LL-37 promotes re-epithelialization and wound closure. It is observed to stimulate angiogenesis (new blood vessel growth) and keratinocyte proliferation, suggesting a physiological role in tissue repair beyond its direct antimicrobial effects.