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The Trypanosoma cruzi NTR (TcNTR) is a type I nitroreductase protein, mitochondrial, oxygen insensitive that have a flavin mononucleotide as prostetic group and uses NADH as an electron donor. Besides TcNTR role in activating the only two prodrugs currently available for the treatment of Chagas disease: benznidazole and Nifurtimox, little information about TcNTR structure and the exact role of this protein has yet been determined. At present, structural studies are highly desirable to improve the understanding on substrate recognition by TcNTR and possibly lead to the design of more specific drugs. In this work, we described the expression, purification and crystallization of TcNTR, Moreover, Molecular modeling, Differential Scanning Calorimetry, Pendand Drop Tensiometry and Electron Paramagnetic Resonance were used to identify the interaction of TcNTR with model membranes. Our results were exploited to hypothesize a possible function of TcNTR in trypanosomatids.
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