LL-37, the only known human cathelicidin which is encoded by the human antimicrobial peptide (CAMP) gene, plays a critical role in protection against bacterial infection.
Here, we optimized a novel gene delivery system based on antimicrobial peptide (LL37) grafted ultra-small gold nanoparticles (AuNPs@LL37, ∼7 nm) for the topical treatment of diabetic wounds with or without bacterial infection.
Neutrophil extracellular traps (NETs) and the cathelicidin antimicrobial peptideLL-37 have been implicated both in defense against bacterial infections and in wound healing process.
The important role of this peptide in infectious diseases is also suggested, however, to date, data relating to LL-37 expression in the course of bacterial infections are far from complete.
Furthermore, Esc(1-21)-1c was more efficacious than Esc(1-21) and LL-37 in protecting host from pulmonary bacterial infection after a single intra-tracheal instillation at a very low dosage of 0.1 mg/kg.
The inhibition of LPS-induced cytokine and adhesion molecule expression in human corneal fibroblasts by LL37 suggests that this peptide might promote the resolution of corneal inflammation associated with bacterial infection.
A better understanding of LL-37's biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.
Collectively, these observations indicate that LL-37 cannot only kill bacteria, but also modulate (suppress) neutrophil apoptosis via the activation of FPRL1 and P2X7 in bacterial infections.