Cathelicidin antimicrobial peptide (CAMP (also known as hCAP18, LL-37))

Cathelicidin antimicrobial peptide (CAMP) is a gene encoding the only human cathelicidin, whose precursor is hCAP18 (or CAP-18), processed to the bioactive peptide LL-37 in humans[2][6]. LL-37 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses, primarily via disruption of pathogen membranes. Besides its direct antimicrobial effects, LL-37 modulates immune responses by acting as a chemoattractant and influencing cytokine release, playing critical roles in inflammation, wound healing, and communication between innate and adaptive immunity[1][5][6]. Expression of CAMP is strongly induced by the active form of vitamin D via the vitamin D receptor, linking its activity to both immune activation and nutritional status. Dysregulation of CAMP/LL-37 has been implicated in infectious diseases, inflammatory disorders, and various cancers—acting as either a tumor suppressor or promoter depending on cellular context[3][4]. Safety concerns for therapeutic use include the peptide's short half-life and dual roles in cancer biology, and there are no currently approved drugs directly targeting CAMP/LL-37, though modulation by vitamin D analogs is under investigation[2][3].

Other names

hCAP18LL-37CAP-18CathelicidinCathelicidin antimicrobial protein

Disruption of microbial membranes; Modulation of immune cell recruitment and cytokine responses; Induction by vitamin D and other immune signaling pathways[1][2][5]