What is it about?
The current study set out to understand the structure-activity relationships of ThyX in Mtb using a combination of cheminformatics and in vitro screening. We report the identification of new Mtb ThyX inhibitors, 2-chloro-3-(4-methanesulfonylpiperazin-1-yl)-1,4-dihydronaphthalene-1,4-dione) and idebenone.
Featured Image
Why is it important?
We show how similarity searching, pharmacophores and machine learning can be used with ThyX. ThyX is an essential thymidylate synthase (TS) that is both mechanistically and structurally unrelated to the analogous human enzyme. We started with napthoquinones and looked at overlap of compounds with GyrX. We had more success with finding new compounds for ThyX than Gyr.
Perspectives
An international collaboration with groups in France, UK, South Africa, Uganda and the USA. What started as from the overlap of napthoquinones having some overlap in activity for ThyX and Gyr lead to a study including computational and experimental testing.
Dr Sean Ekins
Collaborations in Chemistry
Read the Original
This page is a summary of: Predictive modeling targets thymidylate synthase ThyX in Mycobacterium tuberculosis, Scientific Reports, June 2016, Nature,
DOI: 10.1038/srep27792.
You can read the full text:
Contributors
The following have contributed to this page
