Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: A comparative perspective

International Journal of Biological Macromolecules
Karine MinariJúlio C Borges

Abstract

Hsp90s are key proteins in cellular homeostasis since they interact with many client proteins. Several studies indicated that Hsp90s are potential targets for treating diseases, such as cancer or malaria. It has been shown that Hsp90s from different organisms have peculiarities despite their high sequence identity. Therefore, a detailed comparative analysis of several Hsp90 proteins is relevant to the overall understanding of their activity. Accordingly, the goal of this work was to evaluate the interaction of either ADP or ATP with recombinant Hsp90s from different organisms (human α and β isoforms, Plasmodium falciparum, Leishmania braziliensis, yeast and sugarcane) by isothermal titration calorimetry. The measured thermodynamic signatures of those interactions indicated that despite the high identity among all Hsp90s, they have specific thermodynamic characteristics. Specifically, the interactions with ADP are driven by enthalpy but are opposed by entropy, whereas the interaction with ATP is driven by both enthalpy and entropy. Complimentary structural and molecular dynamics studies suggested that specific interactions with ADP that differ from those with ATP may contribute to the observed enthalpies and entropies. Altogethe...Continue Reading

Citations

Feb 13, 2020·Journal of Enzyme Inhibition and Medicinal Chemistry·Fernanda A H BatistaJúlio C Borges
Mar 11, 2021·ACS Infectious Diseases·Tatyana Almeida TavellaFabio Trindade Maranhão-Costa
Apr 16, 2021·International Journal of Biological Macromolecules·Paulo Roberto Dores-SilvaJúlio César Borges
Dec 13, 2019·The Journal of Physical Chemistry. B·Saikat Pal, Sandip Paul
Sep 28, 2021·Biochimica Et Biophysica Acta. Proteins and Proteomics·Noeli Soares Melo SilvaJúlio César Borges

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