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Chem Commun (Camb) ; 53(63): 8878-8881, 2017 Aug 03.
Article in English | MEDLINE | ID: mdl-28737795

ABSTRACT

We discovered a promising metallo-ß-lactamase inhibitor, a DNA nanoribbon, by enzymatic kinetics and isothermal titration calorimetry evaluations. Atomic force microscopy, gel electrophoresis, competitive binding experiments, circular dichroic and thermal denaturation studies suggested that the DNA nanoribbon could bind to the enzyme through a minor groove.


Subject(s)
DNA/pharmacology , Nanotubes, Carbon/chemistry , beta-Lactamase Inhibitors/pharmacology , beta-Lactamases/metabolism , DNA/chemistry , beta-Lactamase Inhibitors/chemistry
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