Ontology highlight
ABSTRACT:
SUBMITTER: Yang H
PROVIDER: S-EPMC6356018 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
Yang Hyunjun H Wierzbicki Michał M Du Bois Derek R DR Nowick James S JS
Journal of the American Chemical Society 20181012 43
This paper describes the X-ray crystallographic structure of a derivative of the antibiotic teixobactin and shows that its supramolecular assembly through the formation of antiparallel β-sheets creates binding sites for oxyanions. An active derivative of teixobactin containing lysine in place of allo-enduracididine assembles to form amyloid-like fibrils, which are observed through a thioflavin T fluorescence assay and by transmission electron microscopy. A homologue, bearing an N-methyl substitu ...[more]