LL-37 is a human cathelicidin-derived antimicrobial peptide (AMP) with broad-spectrum antimicrobial activity and potential applications in combating antibiotic-resistant infections. It is the only cathelicidin-derived AMP in humans and has been extensively studied for its structural, functional, and therapeutic properties. LL-37 is expressed in various tissues and immune cells, and it exhibits antimicrobial, antiviral, anticancer, and anti-amyloidogenic activities. It also plays a role in inflammatory responses, wound healing, and immune modulation. Recent studies have shown that LL-37 can disrupt bacterial membranes through mechanisms such as the toroidal pore model, and it has potential as a therapeutic agent for infections caused by drug-resistant bacteria. Additionally, LL-37 has been implicated in the pathogenesis of amyloid-related diseases, including Alzheimer's disease. The structure of LL-37 is helical and amphipathic, and it can form monomers, dimers, and tetramers in different environments. Its derivatives, such as the core peptide and KR-12, have also been studied for their antimicrobial and therapeutic properties. Solid-state NMR studies have provided insights into the mechanism of LL-37's membrane disruption, suggesting a toroidal pore model. Overall, LL-37 is a promising candidate for the development of new antimicrobial agents and therapies for drug-resistant infections and amyloid-related diseases.LL-37 is a human cathelicidin-derived antimicrobial peptide (AMP) with broad-spectrum antimicrobial activity and potential applications in combating antibiotic-resistant infections. It is the only cathelicidin-derived AMP in humans and has been extensively studied for its structural, functional, and therapeutic properties. LL-37 is expressed in various tissues and immune cells, and it exhibits antimicrobial, antiviral, anticancer, and anti-amyloidogenic activities. It also plays a role in inflammatory responses, wound healing, and immune modulation. Recent studies have shown that LL-37 can disrupt bacterial membranes through mechanisms such as the toroidal pore model, and it has potential as a therapeutic agent for infections caused by drug-resistant bacteria. Additionally, LL-37 has been implicated in the pathogenesis of amyloid-related diseases, including Alzheimer's disease. The structure of LL-37 is helical and amphipathic, and it can form monomers, dimers, and tetramers in different environments. Its derivatives, such as the core peptide and KR-12, have also been studied for their antimicrobial and therapeutic properties. Solid-state NMR studies have provided insights into the mechanism of LL-37's membrane disruption, suggesting a toroidal pore model. Overall, LL-37 is a promising candidate for the development of new antimicrobial agents and therapies for drug-resistant infections and amyloid-related diseases.