AI Article Synopsis
- A series of Schiff bases derived from indoline-2,3-dione were synthesized and tested for their ability to inhibit Mtb gyrase, showing IC(50) values between 50-157 mM for some derivatives.
- The study utilized advanced docking techniques with MOE and Autodock4 software to explore how these compounds interact with the Mtb DNA gyrase A subunit, highlighting the significance of the isatin moiety and side chain in these interactions.
- Among the compounds tested, the benzofuran ring demonstrated the highest inhibitory activity, suggesting potential new leads for creating a novel class of Mtb gyrase inhibitors.
Article Abstract
In the present study a series of Schiff bases of indoline-2,3-dione were synthesized and investigated for their Mtb gyrase inhibitory activity. Promising inhibitory activity was demonstrated with some of these derivatives, which exhibited IC(50) values ranging from 50-157 mM. The orientation and the ligand-receptor interactions of such molecules within the Mtb DNA gyrase A subunit active site were investigated applying a multi-step docking protocol using Molecular Operating Environment (MOE) and Autodock4 docking software. The results revealed the importance of the isatin moiety and the connecting side chain for strong interactions with the enzyme active site. Among the tested compounds the terminal aromatic ring benzofuran showed the best activity. Promising new leads for developing a novel class of Mtb gyrase inhibitors were obtained from Schiff bases of indoline-2,3-dione.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264139 | PMC |
| http://dx.doi.org/10.3390/molecules16097864 | DOI Listing |
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