Fig. 3 | Scientific Reports

Fig. 3

From: Biophysical and transcriptomic characterization of LL-37-derived antimicrobial peptide targeting multidrug-resistant Escherichia coli and ESKAPE pathogens

Fig. 3

Binding selectivity of the peptide for bacterial versus mammalian membrane mimics assessed by SPR and ITC. (A) Surface plasmon resonance (SPR) analysis shows distinct binding profiles of the peptide to lipid-coated sensor chips mimicking bacterial (POPE/POPG) and mammalian (POPC/cholesterol) membranes. A table summarizes the kinetic parameters derived from the fits. Sensorgrams represent the mean values of three independent experiments. (B) Isothermal titration calorimetry (ITC) measurements reveal strong, thermodynamically favorable binding to bacterial-mimicking vesicles, with minimal interaction observed for mammalian-mimicking vesicles. A summary of thermodynamic parameters and binding stoichiometries is provided in the accompanying table. The thermodynamic parameters shown are mean ± SD from three replicates.

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