This review article focuses on the antimicrobial peptide LL-37, a cathelicidin-derived antimicrobial precursor protein (AMP) found in humans. LL-37 is the only cathelicidin AMP in humans and has been extensively studied for its broad-spectrum antimicrobial activity, host defense activities, and potential therapeutic applications. The article highlights the significance of AMPs in combating antibiotic-resistant bacteria and the challenges posed by multi-drug resistant (MDR) and pan-drug resistant (PDR) strains. LL-37's structural diversity, including its monomeric and oligomeric forms, is discussed, along with its ability to form aggregates and oligomers in different environments. The review also explores LL-37's role in modulating inflammatory responses, wound healing, and its potential anticancer and anti-amyloidogenic properties. Additionally, the article delves into the structural studies of LL-37, including its interactions with lipid membranes and the mechanisms of membrane disruption. The review aims to provide a comprehensive understanding of LL-37's structures, biophysical properties, and functional roles, laying the groundwork for future research and the development of novel LL-37-based molecules.This review article focuses on the antimicrobial peptide LL-37, a cathelicidin-derived antimicrobial precursor protein (AMP) found in humans. LL-37 is the only cathelicidin AMP in humans and has been extensively studied for its broad-spectrum antimicrobial activity, host defense activities, and potential therapeutic applications. The article highlights the significance of AMPs in combating antibiotic-resistant bacteria and the challenges posed by multi-drug resistant (MDR) and pan-drug resistant (PDR) strains. LL-37's structural diversity, including its monomeric and oligomeric forms, is discussed, along with its ability to form aggregates and oligomers in different environments. The review also explores LL-37's role in modulating inflammatory responses, wound healing, and its potential anticancer and anti-amyloidogenic properties. Additionally, the article delves into the structural studies of LL-37, including its interactions with lipid membranes and the mechanisms of membrane disruption. The review aims to provide a comprehensive understanding of LL-37's structures, biophysical properties, and functional roles, laying the groundwork for future research and the development of novel LL-37-based molecules.