Design, synthesis and evaluation of novel 2,5,6-trisubstituted benzimidazoles targeting FtsZ as antitubercular agents

Bioorg Med Chem. 2014 May 1;22(9):2602-12. doi: 10.1016/j.bmc.2014.03.035. Epub 2014 Apr 1.

Abstract

Filamenting temperature-sensitive protein Z (FtsZ), an essential cell division protein, is a promising target for the drug discovery of new-generation antibacterial agents against various bacterial pathogens. As a part of SAR studies on benzimidazoles, we have synthesized a library of 376 novel 2,5,6-trisubstituted benzimidazoles, bearing ether or thioether linkage at the 6-position. In a preliminary HTP screening against Mtb H37Rv, 108 compounds were identified as hits at a cut off concentration of 5 μg/mL. Among those hits, 10 compounds exhibited MIC values in the range of 0.63-12.5 μg/mL. Light scattering assay and TEM analysis with the most potent compound 5a clearly indicate that its molecular target is Mtb-FtsZ. Also, the Kd of 5a with Mtb-FtsZ was determined to be 1.32 μM.

Keywords: Antibacterial; Benzimidazole; FtsZ; Tuberculosis.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Antitubercular Agents / chemical synthesis*
  • Antitubercular Agents / chemistry
  • Antitubercular Agents / toxicity
  • Archaeal Proteins / antagonists & inhibitors
  • Archaeal Proteins / metabolism*
  • Benzimidazoles / chemical synthesis
  • Benzimidazoles / chemistry*
  • Benzimidazoles / toxicity
  • Cell Survival / drug effects
  • Chlorocebus aethiops
  • Drug Design*
  • Microbial Sensitivity Tests
  • Mycobacterium tuberculosis / drug effects
  • Mycobacterium tuberculosis / metabolism
  • Structure-Activity Relationship
  • Vero Cells

Substances

  • Antitubercular Agents
  • Archaeal Proteins
  • Benzimidazoles
  • FtsZ protein, Methanococcus jannaschii