Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy
| Autor: | Phoebe Do Carmo Silva, Shaun W. Lee, Victoria A. Ploplis, Mayland Chang, Rashna D. Balsara, Alejandro J. Gonzalez, Jeshina Janardhanan, Francisco R. Fields, Jessica N Ross, Francis J. Castellino, Melanie Clifford, Ilona P. Foik, J. Mark Sutton, Charlotte K. Hind, Henry M. Vu, Veronica R. Kalwajtys, Tam T. T. Bui, A. James Mason, Albert Siryaporn, Giorgia Manzo |
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| Rok vydání: | 2020 |
| Předmět: |
Pharmacology
chemistry.chemical_classification biology Chemistry medicine.drug_class Antimicrobial peptides Antibiotics synergy Peptide biology.organism_classification Antimicrobial bacteriocins antimicrobial peptides Membrane Biochemistry Bacteriocin 5.1 Pharmaceuticals medicine Pharmacology (medical) Antimicrobial Resistance Development of treatments and therapeutic interventions Infection Bacteria |
| Zdroj: | ACS pharmacology & translational science, vol 3, iss 3 ACS Pharmacol Transl Sci |
| Popis: | [Image: see text] 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. |
| Databáze: | OpenAIRE |
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