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Analyzing interaction of rhodacyanine inhibitor MKT-077 with Plasmodium falciparum HSP70 nucleotide binding domains

Nainani, C.; Upadhyay, V.; Singh, B.; Sandhu, K. K.; Kaur, S.; Hora, R.; Mishra, P. C.

2023-07-29 bioinformatics
10.1101/2023.07.27.550796 bioRxiv
Show abstract

MKT-077 and its derivatives are rhodacyanine inhibitors that hold potential in treatment of cancer, neurodegenerative diseases and malaria. These allosteric drugs act by inhibiting the ATPase action of heat shock proteins of 70kDa (HSP70). MKT-077 accumulates in the mitochondria and displays differential activity against HSP70 homologs. The four Plasmodium falciparum HSP70s (PfHSP70) are present at various subcellular locations to perform distinct functions. In the present study, we have used bioinformatics tools to understand interactions between MKT-077 and PfHSP70s. Nature of the identified interactions is primarily hydrophobic with different PfHSP70 homologs showing variable propensity to bind MKT-077. Our molecular docking approach has helped us to predict the binding pocket and specific residues on PfHSP70s that are involved in interacting with MKT-077. Information derived from this article may form the foundation for design and development of MKT-077 based drugs against malaria.

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