The final stage of the in silico study consisted of molecular docking studies at the active site of the protein Trypanothione reductase of T. cruzi , with molecules NF-85, 91, 150, 246 and 279. The selection of the crystal of the protein 1BZL was considered to have been obtained by X-ray diffraction, with a resolution of the crystal structure of 2.40 Å. Likewise, the parameters of the validation report of the structure are within suitable ranges and is co-crystallized with trypanothione its endogenous ligand at the most likely binding site.