Production of recombinant mitochondrial Hsp70 chaperone of Plasmodium falciparum aiming structural characterization and functional

• Grant number: 16/20405-3
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• Start date: January 01, 2017
• End date: December 31, 2017
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Julio Cesar Borges
• Grantee: Ana Beatriz de Freitas Barranco
• Host Institution: Instituto de Química de São Carlos (IQSC). Universidade de São Paulo (USP). São Carlos , 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

Molecular chaperones are proteins that by the interaction with others proteins help them to achieve their native structure successfully and prevent aggregation. Among the known molecular chaperones, Hsp70 are ubiquitous proteins highly conserved and essential for the control of protein folding, indiscriminately interacting with newly synthesized proteins, unfolded and partially folded proteins. Therefore, Hsp70 are vital to the cell, since its inactivation leads to the suppression of growth of organisms, such as protozoa, thus preventing the progression of its life cycle. For that reason, the knowledge of the native structure and functional mechanism of this protein are extremely valuable since it is an important therapeutic target. The aim of this research project is to obtain structural and functional information of mitochondrial Hsp70 of Plasmodium falciparum (PfmtHsp70), continuing the project already under development by the applicant. (AU)