Thermodynamic characterization of Hsp90 interaction with other proteins

• Grant number: 16/14503-2
• Support type: Scholarships in Brazil - Post-Doctorate
• Effective date (Start): September 01, 2016
• Effective date (End): July 31, 2018
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Carlos Henrique Inacio Ramos
• Grantee: Maria Luiza Caldas Nogueira
• Home Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• Associated research grant: 12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis, AP.TEM

Abstract

The study of the interaction between Hsp90 and chaperones and the search for small molecules that can modulate Hsp90 function are of utmost importance for the advancement of scientific knowledge on various cellular mechanisms. Also, it may improve the search for new drugs to increase recombinant protein production and to decrease aggregates in pathological conditions. Full characterization of the interactions requires molecular biophysical studies to assess the relationship between structure and function of proteins. The quantification of the binding affinity number of binding sites and the binding thermodynamics, that give us information about the energetic forces that generate biomolecular interactions will also be investigated. This project aims to explore spectroscopic, hydrodynamic and microcalorimetry for thermodynamic characterization of interactions between the Hsp90-Hsp70 chaperone system and between this system and other proteins. (AU)