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Characterization of Ribosomal Binding and Antibacterial Activities Using Two Orthogonal High-Throughput Screens
Author(s) -
Ada King,
Derrick Watkins,
Sunil Kumar,
Nihar Ranjan,
Changjun Gong,
Jarred M. Whitlock,
Dev P. Arya
Publication year - 2013
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.00671-13
Subject(s) - antibacterial activity , neomycin , ribosomal rna , ribosomal protein , chemistry , biology , biochemistry , rna , bacteria , antibiotics , ribosome , genetics , gene
We report here the affinity and antibacterial activity of a structurally similar class of neomycin dimers. The affinity of the dimer library for rRNA was established by using a screen that measures the displacement of fluorescein-neomycin (F-neo) probe from RNA. A rapid growth inhibition assay using a single drug concentration was used to examine the antibacterial activity. The structure-activity relationship data were then rapidly analyzed using a two-dimensional ribosomal binding-bacterial inhibition plot analysis.

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