<unk>  antimicrobial peptide (CAMP) is a polypeptide that is primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs); in humans, the CAMP gene encodes the peptide precursor CAP-18 (18 kDa), which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37. LL-37 is the only peptide in the<unk>  family found in the human body.<unk>  peptides are dual-natured molecules called amphiphiles: one end of the molecule is attracted to water and repelled by fats and proteins, and the other end is attracted to fat and proteins and repelled by water. Members of this family react to pathogens by disintegrating, damaging, or puncturing cell membranes.<unk> s thus serve a critical role in mammalian innate immune defense against invasive bacterial infection. The<unk>  family of peptides are classified as antimicrobial peptides (AMPs). The AMP family also includes the defensins. Whilst the defensins share common structural features,<unk> -related peptides are highly heterogeneous. Members of the<unk>  family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable<unk>  peptide domain.<unk>  peptides have been isolated from many different species of mammals.<unk> s are mostly found in neutrophils, monocytes, mast cells, dendritic cells and macrophages after activation by bacteria, viruses, fungi, parasites or the hormone 1,25-D, which is the hormonally active form of vitamin D. They have been found in some other cells, including epithelial cells and human keratinocytes.
Cathelicidin
Fibrinolysin
Peroxin-7
Kaliotoxin
Staphylotoxin
Cyanotoxin
Eoxin
Tetanospasmin