CHAPTER 14: Heat-shock Protein 90 as an Antimalarial Target
Published:23 Oct 2013
A. K. Rochani, M. Singh, and U. Tatu, in Inhibitors of Molecular Chaperones as Therapeutic Agents, ed. T. D. Machajewski and Z. Gao, The Royal Society of Chemistry, 2013, pp. 379-391.
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Malaria is a communicable infectious disease that has affected many tropical countries. Fighting malaria has been a major socio-economic problem. In spite of more than a century old fight against the infection, today we have only six highly potent scaffolds that provide therapeutic solutions for malaria. Generics of these molecules have been made available to provide healthcare support to endemic regions but the resistance to these drugs has been emerging simultaneously. Hence malaria has become a priority disease in the healthcare segment. It is observed that during the malaria infection combating stress is the primary requirement of the Plasmodium parasite. One of the molecular chaperones, namely heat-shock protein 90 (Hsp90), helps the parasite to cope with this stress response and this ultimately helps in establishing infection. Inhibition of this molecular chaperone causes stage-specific arrest in parasite growth. This chapter sheds light on the path of discovery of PfHsp90 as novel drug target for malaria and approaches for development of PfHsp90-targeted antimalarial therapy.