Antimicrobial peptides derived from the SPLUNC1 protein perturb bacterial and eukaryotic lipid model membranes

SPLUNC1 (short palate lung and nasal epithelial clone 1) is a multifunctional host defense protein found in the human respiratory tract that possesses antimicrobial properties. Through modification of the 4th alpha helical motif of the protein, five novel antimicrobial peptides (AMPs) were designed with different lengths, charges, hydrophobicities (H) and hydrophobic moments (μH). The goal of this study was to compare the biological activities of these AMPs by means of testing against paired clinical isolates of the Gram-negative (G(-)) bacteria Klebsiella pneumoniae, obtained from twelve patients before and after colistin treatments (half susceptible and half resistant to colistin).