| Autor: |
Mali G; Department of Chemistry, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India. rd.erande@iitj.ac.in., Kumar Yadav V; Department of Bioscience & Bioengineering, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India., Priya H; Department of Chemistry, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India. rd.erande@iitj.ac.in., Shukla M; Department of Bioscience & Bioengineering, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India., Pandey P; Department of Chemistry, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India. rd.erande@iitj.ac.in., Kumar A; Department of Chemistry and Nano Science, Ewha Womans University, Seoul 03760, Korea., Paranjothy M; Department of Chemistry, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India. rd.erande@iitj.ac.in., Bhattacharyya S; Department of Bioscience & Bioengineering, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India., Erande RD; Department of Chemistry, Indian Institute of Technology Jodhpur, Jodhpur 342037, Rajasthan, India. rd.erande@iitj.ac.in. |
| Abstrakt: |
Lewis-acid cascade reactions promoted by BF 3 ·OEt 2 are reported for the synthesis of highly substituted pyrrolo[1,2- a ]indoles and congeners of benzofuro[2,3- b ]indoles. These reactions are highly regio- and diastereoselective towards generating up to five contiguous stereogenic centers, including two vicinal quaternary centers. Furthermore, an established cascade approach and the mechanism proposed herein are well supported by quantum chemistry calculations. In addition, a self-dimerization intermediate was trapped and isolated to establish a strategy for potential access to both pyrrolo and benzo indole derivatives, leaving sufficient freedom for broadening. Furthermore, in-silico molecular docking and all atomistic molecular dynamic (MD) simulation analysis suggests that the synthesized pyrrolo[1,2- a ]indole derivatives stably bind at the active site of the mycobacterial secreted tyrosine phosphatase B (MptpB) enzyme, an emerging anti-mycobacterial drug target. Deep learning-based affinity predictions and MMPBGBSA-based energy calculations of the docked poses are presented herein. |
