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- W2524034808 abstract "Significance The increasing development of antimicrobial resistance is a major global concern, and there is an urgent need for the development of new antibiotics. We show that the antimicrobial lipopeptide tridecaptin A 1 selectively binds to the Gram-negative analogue of peptidoglycan precursor lipid II, disrupting the proton motive force and killing Gram-negative bacteria. We present an example of the selective targeting of Gram-negative lipid II and a binding mode to this peptidoglycan precursor. No persistent resistance develops against tridecaptin A 1 in Escherichia coli cells exposed to subinhibitory concentrations of this peptide during a 1-mo period. This study showcases the excellent antibiotic properties of the tridecaptins in an age where new antibiotics that target Gram-negative bacteria are desperately needed." @default.
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- W2524034808 date "2016-09-29" @default.
- W2524034808 modified "2023-10-15" @default.
- W2524034808 title "Antimicrobial lipopeptide tridecaptin A <sub>1</sub> selectively binds to Gram-negative lipid II" @default.
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- W2524034808 doi "https://doi.org/10.1073/pnas.1608623113" @default.
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