- Main
Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy
- Fields, Francisco R;
- Manzo, Giorgia;
- Hind, Charlotte K;
- Janardhanan, Jeshina;
- Foik, Ilona P;
- Do Carmo Silva, Phoebe;
- Balsara, Rashna D;
- Clifford, Melanie;
- Vu, Henry M;
- Ross, Jessica N;
- Kalwajtys, Veronica R;
- Gonzalez, Alejandro J;
- Bui, Tam T;
- Ploplis, Victoria A;
- Castellino, Francis J;
- Siryaporn, Albert;
- Chang, Mayland;
- Sutton, J Mark;
- Mason, A James;
- Lee, Shaun
- et al.
Published Web Location
https://doi.org/10.1021/acsptsci.0c00001Abstract
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.
Many UC-authored scholarly publications are freely available on this site because of the UC's open access policies. Let us know how this access is important for you.
Main Content
Enter the password to open this PDF file:
-
-
-
-
-
-
-
-
-
-
-
-
-
-