Activity and Synergy of Cu-ATCUN Antimicrobial Peptides

Antibiotic resistance demands innovative strategies and therapies. The pairs of antimicrobial peptides tested in this work show broad-spectrum synergy and are capable of interacting with diverse bacterial membranes. In most cases, the ATCUN motif enhanced the activity of peptides tested in combination. Our studies also show CP10A to be a multifaceted peptide, displaying both cell membrane and intracellular activity and acting as a chameleon, improving the activity of other peptides as needed. The results of the synergy experiments demonstrate the importance of varied modes of action and how these changes can affect the ability to combat pathogens, while also illustrating the value of the metal-binding domain in enhancing the activity of antimicrobial peptides in combination.

Automated summary

Antibiotic resistance calls for innovative strategies and treatments. The tested antimicrobial peptides in this study exhibited broad-spectrum synergy and the ability to interact with various bacterial membranes. In most cases, the presence of the ATCUN motif enhanced the activity of the combined peptides. Additionally, the multifaceted peptide CP10A was found to have both cell membrane and intracellular activity, acting as a chameleon to enhance the activity of other peptides when needed. The results highlight the importance of diverse modes of action and the value of the metal-binding domain in enhancing the activity of antimicrobial peptides in combination.