| Literature DB >> 32566907 |
Francisco R Fields1,2,3, Giorgia Manzo4, Charlotte K Hind5, Jeshina Janardhanan6, Ilona P Foik7, Phoebe Do Carmo Silva5, Rashna D Balsara6,8, Melanie Clifford5, Henry M Vu1,8, Jessica N Ross1,2, Veronica R Kalwajtys1, Alejandro J Gonzalez1, Tam T Bui9, Victoria A Ploplis6,8, Francis J Castellino6,8, Albert Siryaporn7,10, Mayland Chang3,6, J Mark Sutton5, A James Mason4, Shaun Lee1,2,3.
Abstract
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 pore-formation through rational peptide design and increasing the utility of novel antimicrobial peptides by exploiting synergy.Year: 2020 PMID： 32566907 PMCID： PMC7296547 DOI： 10.1021/acsptsci.0c00001
Source DB: PubMed Journal: ACS Pharmacol Transl Sci ISSN： 2575-9108