hCAP18LL37

hCAP18LL37, also known as LL-37, is a human antimicrobial peptide derived from the cathelicidin family. It is encoded by the CAMP (cathelicidin antimicrobial peptide) gene. LL-37 is produced by various cell types, including epithelial cells, neutrophils, and macrophages, and plays a significant role in the innate immune system.

As a cationic peptide, LL-37 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and enveloped viruses. Its mechanism involves disrupting microbial cell membranes, leading to cell death. Beyond its antimicrobial properties, LL-37 influences immune responses by modulating inflammatory processes, promoting wound healing, and inducing chemotaxis of immune cells such as dendritic cells and T lymphocytes.

Structurally, LL-37 is a 37-amino acid peptide that adopts an alpha-helical conformation, which is essential for its functional activity. Its expression is regulated by various factors, including microbial infection and inflammatory cytokines, and its levels can be elevated in certain skin conditions and inflammatory diseases.

Research indicates that LL-37 contributes to host defense but may also be involved in pathological inflammation if dysregulated. It has been studied for potential therapeutic applications, including antimicrobial treatments, wound healing enhancement, and modulation of immune responses in diseases like psoriasis, sepsis, and cystic fibrosis.

Overall, hCAP18LL37 is an integral component of innate immunity, with diverse roles in antimicrobial defense, immune regulation, and tissue repair. Continuous research aims to better understand its mechanisms and therapeutic potential.