Malaria is one of the world’s most devastating diseases, infecting well over 300 million people annually and killing between 2 and 3 million worldwide. Increasing parasite resistance to many existing drugs is exacerbating disease. Resistance to commonly used malarial drugs is increasing the need to develop new drugs urgently. Due to the slow pace and substantial costs of new drug development, repurposing of old drugs which is recently increasingly becoming an attractive proposition of highly efficient and effective way of drug discovery led us to study the drug rifampicin for this purpose. The present paper aims to investigate the route of Plasmodium falciparum apicoplast-targeted proteins that putatively encode β subunits of RNA polymerase with an objective to develop an effective antimalarial drug. Homology searching for conserved binding site to the rifampicin drug and the functional analysis of rpoB gene were done. Multiple Sequence alignment analysis of rpoB was compared with that in E.coli – rpoB and M. tuberculosis – rpoB. Docking studies of Rifampicin – rpoB complex was also done for finding binding affinity. The results of computational studies showed that rifampicin is a potential drug for malaria.

One-pot, multicomponent H2O2-HCl catalyzed system was employed for the synthesis of a series of benzazepine compounds. The implemented procedure oxidized the carbon-nitrogen bonds and produced benzazepines, while integrating diamines and substituted ketone. The advantage of the exercised synthetic route was that the reaction was water mediated and the completion time was quite reduced compared to the time required by conventional methods