Abstract
ONE OF THE OLDEST ANTIbacterials has finally been caught in the act: Using high-resolution nuclear magnetic resonance spectroscopy Dutch researchers freeze-framed the binding action of the peptide nisin with lipid II, a bacterial cell wall precursor { Nat. Struct. Mol. Biol. , published online Sept. 12, http://dx.doi.org/10.1038/nsmb 830}. Understanding nisin's binding should give drug-makers ideas for creating antibiotics to which bacteria are less likely to develop resistance. Nisin is one of a class of antibacterials called lantibiotics, and it has intrigued scientists for along time. A natural antibiotic created by some bacteria to fight others, it was first discovered in milk. It has been used as a food preservative in cheese and dairy products for about 40 years in more than 80 countries, yet resistance to the peptide is rare. The nisin-lipid II binding structure reveals why. Researchers at Utrecht University led by spectroscopy Robert Kaptein and biochemist Eefjan Breukink, took an ...
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