Fragment-Based Optimized EthR Inhibitors with in Vivo Ethionamide Boosting Activity

ACS Infect Dis. 2020 Mar 13;6(3):366-378. doi: 10.1021/acsinfecdis.9b00277. Epub 2020 Mar 2.

Abstract

Killing more than one million people each year, tuberculosis remains the leading cause of death from a single infectious agent. The growing threat of multidrug-resistant strains of Mycobacterium tuberculosis stresses the need for alternative therapies. EthR, a mycobacterial transcriptional regulator, is involved in the control of the bioactivation of the second-line drug ethionamide. We have previously reported the discovery of in vitro nanomolar boosters of ethionamide through fragment-based approaches. In this study, we have further explored the structure-activity and structure-property relationships in this chemical family. By combining structure-based drug design and in vitro evaluation of the compounds, we identified a new oxadiazole compound as the first fragment-based ethionamide booster which proved to be active in vivo, in an acute model of tuberculosis infection.

Keywords: Ethionamide booster; Fragment-based drug design; Tuberculosis; in vivo POC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antitubercular Agents / chemistry
  • Antitubercular Agents / pharmacology*
  • Crystallography, X-Ray
  • Drug Design*
  • Drug Discovery
  • Ethionamide / chemistry
  • Ethionamide / pharmacology*
  • Female
  • Mice
  • Mice, Inbred BALB C
  • Mycobacterium tuberculosis / drug effects*
  • Oxadiazoles / chemistry
  • Oxadiazoles / isolation & purification
  • Oxadiazoles / pharmacology*
  • Repressor Proteins / antagonists & inhibitors*
  • Structure-Activity Relationship
  • Tuberculosis / drug therapy

Substances

  • Antitubercular Agents
  • EthR protein, Mycobacterium tuberculosis
  • Oxadiazoles
  • Repressor Proteins
  • Ethionamide