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

ABSTRACT: The emergence of multidrug-resistant (MDR) bacterial pathogens is an alarming global health threat that demands new therapeutic strategies beyond conventional antibiotics. Here, we present a rationally designed antimicrobial peptide (AMP) derived from mammalian cathelicidins and defensins that selectively targets bacterial membranes with low cytotoxicity toward mammalian cells. Circular dichroism spectroscopy revealed that the peptide adopts an α-helical conformation upon membrane interaction, a key feature of its mechanism. Surface plasmon resonance and isothermal titration calorimetry demonstrated high-affinity and selective binding to bacterial lipid membranes. Functionally, the peptide was strongly bactericidal against clinical MDR Escherichia coli (E. coli) and clinically important ES

SUBMITTER: Eladl O 

PROVIDER: S-EPMC12533254 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature