LL-37

Szarszoń et al. (2026) characterized Cu(II) and Zn(II) coordination chemistry of LL-37, its C-terminal fragment DF-12, and an all-D stereoisomer analogue (df-12) using potentiometric, spectroscopic, and microbiological methods. At physiological pH, both metal ions bound through the N-terminal amino group and a carboxylate donor, with divergent coordination pathways at higher pH. LL-37 retained its α-helical conformation upon metal binding. In antimicrobial and antibiofilm plate assays, full-length LL-37 displayed the broadest activity spectrum among the tested peptides. Truncation altered antibacterial assay outcomes, although DF-12 and df-12 showed measurable antifungal and antibiofilm activity with low cytotoxicity in the cell models tested [42708248].