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The rise of antimicrobial resistance requires novel antibiotics with unexploited modes of action. Promising templates could be antibiotics that target Lipid II, known as the Achilles' heel of bacteria, at an irreplaceable pyrophosphate group. Such antibiotics, like nisin, plectasin, or teixobactin [1-3] would kill the most refractory pathogens without causing resistance. However, due to the challenge of studying small membrane-embedded drug-receptor complexes in native conditions, the structural correlates of the pharmaceutically relevant binding modes are unknown.
Here, using modern solid-state NMR methods that enable atomic-resolution studies in native bacterial membranes, we report on the physiologically relevant binding modes of several Lipid II-binding antibiotics.[4-5]

[1] Breukink et al, Science 2006
[2] Schneider et al., Science 2010
[3] Ling et al., Nature 2015
[4] Medeiros¬-Silva et al., Nature Communications 2018 [5] Shukla et al., Nature Communications 2020

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