| Structural highlights
Publication Abstract from PubMed
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.
Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy.,Fields FR, Manzo G, Hind CK, Janardhanan J, Foik IP, Carmo Silva PD, Balsara RD, Clifford M, Vu HM, Ross JN, Kalwajtys VR, Gonzalez AJ, Bui TT, Ploplis VA, Castellino FJ, Siryaporn A, Chang M, Sutton JM, Mason AJ, Lee S ACS Pharmacol Transl Sci. 2020 Feb 21;3(3):418-424. doi:, 10.1021/acsptsci.0c00001. eCollection 2020 Jun 12. PMID:32566907[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fields FR, Manzo G, Hind CK, Janardhanan J, Foik IP, Carmo Silva PD, Balsara RD, Clifford M, Vu HM, Ross JN, Kalwajtys VR, Gonzalez AJ, Bui TT, Ploplis VA, Castellino FJ, Siryaporn A, Chang M, Sutton JM, Mason AJ, Lee S. Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy. ACS Pharmacol Transl Sci. 2020 Feb 21;3(3):418-424. doi:, 10.1021/acsptsci.0c00001. eCollection 2020 Jun 12. PMID:32566907 doi:http://dx.doi.org/10.1021/acsptsci.0c00001
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