Benzothiazole analogs as potential anti-TB agents: computational input and molecular dynamics

J Biomol Struct Dyn. 2019 Apr;37(7):1830-1842. doi: 10.1080/07391102.2018.1470035. Epub 2018 May 16.

Abstract

Biotin is very important for the survival of Mycobacterium tuberculosis. 7,8-Diamino pelargonic acid aminotransaminase (DAPA) is a transaminase enzyme involved in the biosynthesis of biotin. The benzothiazole title compounds were investigated for their in vitro anti-tubercular activity against two tubercular strains: H37Rv (ATCC 25,177) and MDR-MTB (multidrug-resistant M. tuberculosis, resistant to isoniazid, rifampicin, and ethambutol) by an agar incorporation method. The possible binding mode and predicted affinity were computed using a molecular docking study. Among the synthesized compounds in the series, the title compound {2-(benzo[d]thiazol-2-yl-methoxy)-5-fluorophenyl}-(4-chlorophenyl)-methanone was found to exhibit significant activity with minimum inhibitory concentrations of 1 μg/mL and 2 μg/mL against H37Rv and MDR-MTB, respectively; this compound showed the highest binding affinity (-24.75 kcal/mol) as well.

Keywords: Benzothiazole; DAPA: 7,8-diamino pelargonic acid aminotransferase; H37Rv; MDR-MTB; MDR-MTB: multidrug-resistant strains of; MIC: minimum inhibitory concentration; PLP: Pyridoxal phosphate; SAM: S-adenosylmethionine; XDR-MTB: extensively drug-resistant; minimum inhibitory concentration; single crystal X-ray studies.

MeSH terms

  • Antitubercular Agents / chemistry*
  • Antitubercular Agents / pharmacology
  • Benzothiazoles / chemistry*
  • Benzothiazoles / pharmacology
  • Binding Sites
  • Hydrogen Bonding
  • Microbial Sensitivity Tests
  • Molecular Docking Simulation*
  • Molecular Dynamics Simulation*
  • Molecular Structure
  • Mycobacterium tuberculosis / drug effects
  • Protein Binding
  • Structure-Activity Relationship

Substances

  • Antitubercular Agents
  • Benzothiazoles