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Synthetic antimicrobial peptide tuning permits membrane disruption and interpeptide synergy

Research output: Contribution to journalArticle

Francisco Fields, Giorgia Manzo, Charlotte K. Hind, Jeshina Janardhanan, Ilona Foik, Phoebe Do Carmo Silva, Rashna Balsara, Melanie Clifford, Henry Vu, Jessica Ross, Veronica Kalwajtys, Alejandro Gonzalez, Tam Bui, Victoria Ploplis, Francis Castellino, Albert Siryaporn, Mayland Chang, J. Mark Sutton, James Mason, Shaun Lee

Original languageEnglish
JournalACS Pharmacology & Translational Science
Publication statusE-pub ahead of print - 21 Feb 2020

King's Authors


The ribosomally produced antimicrobial peptides of bacteria (bacteriocins) represent an unexplored source of membrane-active antibiotics. We designed a library of linear peptides from a circular bacteriocin and show that pore-formation dynamics in bacterial membranes are tunable via selective amino acid substitution. We observed antibacterial interpeptide synergy indicating that fundamentally altering interactions with the membrane enables synergy. Our findings suggest an approach for engineering poreformation through rational peptide design and increasing the utility of novel antimicrobial peptides by exploiting synergy.

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