NMR structure determination of the Trypanosoma cruzi P21 protein

• Grant number: 14/02192-7
• Support type: Scholarships abroad - Research Internship - Doctorate (Direct)
• Effective date (Start): April 01, 2014
• Effective date (End): March 31, 2015
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal researcher: Claudia Elisabeth Munte
• Grantee: Francesco Brugnera Teixeira
• Supervisor abroad: Hans Robert Kalbitzer
• Home Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
• Research place: University of Regensburg, Germany
• Associated to the scholarship: 12/21153-7 - Structural studies on Trypanosoma cruzi P21 protein as a strategy for Chagas Disease treatment, BP.DD

Abstract

This project aims to solve the tridimensional structure of the P21 protein of T. cruzi using multidimensional, high-resolution NMR spectroscopy, and to investigate its interaction with the CXCR4 chemokine receptor. To achieve this goal, the NMR spectra necessary to finalize the complete assignments, and the required NOESY-type spectra for structure calculation we will acquired in an 800 MHz spectrometer equipped with a TCI cryoprobe. The assignment of the NOEs for the resolution of the structure is expected to be performed using the KNOWNOE module of the software AUREMOL. Because P21 is predicted to be an all-alpha protein, it represents a new level of challenge for the software, and an interactive work-together with the software developers will be essential for this work to be successful. Additionally, the interaction between the protein P21 and the N-terminal CXCR4 peptide will be investigated by acquiring 15N-HSQC NMR spectra. (AU)