Analysis Biomolecular Interactions of αMI and LL-37 by BLI (CAT#: STEM-MB-0169-CJ)

Introduction

Cathelicidins are a family of anti-microbial proteins widely found in many vertebrate species. hCAP-18 is the only human cathelicidin. After release by proteolysis, the C-terminal 37 amino acids of hCAP-18 form the anti-microbial peptide LL-37, named after its two N-terminal leucine residues. LL-37 destroys the integrity of the cell membrane of pathogens, including bacteria, fungi and viruses. More recently, it has become clear that LL-37 modulates leukocyte responses. In vivo, LL-37 is degraded by several serine proteases, which generate a number of smaller fragments with anti-microbial activity. These fragments tend to carry a higher anti-microbial potency, while their pro-inflammatory effects are weaker. Two short LL-37 fragments, usually referred to as the “core peptides,” FK-13 and KR-12, have been identified as the minimal fragments with anti-microbial activity to human immunodeficiency virus and Escherichia coli.