Dimerization of cell-penetrating buforin II enhances antimicrobial properties

Abstract Antimicrobial peptides (AMPs) that selectively permeabilize bacterial membranes are promising alternatives to conventional antibiotics. Dimerization of AMP is considered an attractive strategy enhance antimicrobial and membrane-lytic activity, but it also increases undesired hemolytic cytotoxic activity. Here, we prepared Lys-linked homodimers membrane-permeabilizing magainin II cell-penetrating buforin II. did not significantly alter conformational behavior, had a substantial impact on properties. We found while the dimer showed increased effects, conferred much greater antibacterial potency without exhibiting Interestingly, was highly effective against several antibiotic-resistant isolates. Membrane permeabilization experiments indicated rapidly disrupted both anionic zwitterionic membranes, whereas membranes. Like monomeric form, efficiently translocated across lipid bilayers. Therefore, our results suggest dimerization only disrupts membrane, translocates membrane target intracellular components, resulting in propose targeting AMPs may present superior for therapeutic control pathogenic bacteria.