LL-37 (also known as the last 37 amino acids of hCAP-18) is a positively charged, spiral-shaped (α-helical) peptide of 37 amino acids. It is cut from its precursor protein hCAP18 by neutrophil elastase and cathepsin G (protein-cutting enzymes from white blood cells). LL-37 kills germs in several ways: it forms membrane-spanning pores (holes) that break open their outer skin, it soaks up lipopolysaccharides and lipoteichoic acids (toxins from bacterial walls), it attacks bacterial nucleic acids (DNA and RNA) inside the cell, and it triggers autophagy (the cell's self-cleaning process). Beyond killing germs, LL-37 tunes the immune system through TLR9 signaling (a germ-sensing pathway), draws immune cells to a spot (chemotaxis) by activating formyl peptide receptor-like 1 (FPRL-1, also called the lipoxin A4 receptor), boosts angiogenesis (new blood vessel growth) and wound healing, and holds back excessive inflammation by raising IL-10 (an anti-inflammatory signal).