Characterization of ribosomal binding and antibacterial activities using two orthogonal high-throughput screens

Antimicrob Agents Chemother. 2013 Oct;57(10):4717-26. doi: 10.1128/AAC.00671-13. Epub 2013 Jul 15.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / pharmacology*
  • Enterobacter cloacae / drug effects
  • Microbial Sensitivity Tests
  • Molecular Structure
  • Neomycin / chemistry
  • Neomycin / pharmacology
  • Pseudomonas aeruginosa / drug effects
  • Ribosomes / chemistry*
  • Serratia marcescens / drug effects
  • Staphylococcus aureus / drug effects
  • Structure-Activity Relationship

Substances

  • Anti-Bacterial Agents
  • Neomycin