The protein folding is critical in cellular physiology, constituting a self-organizing process in which the tertiary structure of a polypeptide chain is dictated by its amino acid sequence. Under conditions of stress, Hsp (heat shock proteins) maintains cellular homeostasis assisting in the correct folding of nascent protein chains, preventing protein aggregation and promoting the selective degradation of proteins poorly folded. The Hsp90 chaperones are proteins ATP-dependent, evolutionarily conserved and involved in the stabilization and activation of more than 200 proteins known as clients proteins. The functions of chaperones are not limited to assist the folding of nascent proteins, but they are also involved in the regulation of gene expression and signaling events. In the case of intracellular parasites the role of chaperones goes beyond maintaining homeostasis protein, they are also involved in different processes related to the development and pathogenesis of these organisms. The ability of Hsp90 to affect important cellular transformations is very exploited by intracellular protozoa such as leishmania and plasmodium. These parasites, which can cause malaria and leishmaniasis in the human host, use the Hsp90 to trigger transitions among its various stages. Therefore the Hsp90 are potential targets for drug development since its inhibition affects several cycles and intracellular signaling pathways in humans and protozoa parasitizing man. Although Hsp90 parasites have shown important therapeutic targets in the search for drugs to treat these parasites, the high similarity between Hsp90 belonging to parasites and to man, arises as a point of attention in this approach. Thus, the aim of this study is to explore and identify molecules capable of causing inhibition of Hsp90 from leishmania and plasmodium, without affecting the activity of human Hsp90.
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