Abstract
Objective: To evaluate the bioactive activity of desloratadine through in silico studies by molecular doping in organisms of the genus Schistosoma. Methods: For the study, 3D proteins from cathepsin B1 (2cb1), purine nucleoside phosphorylase (pnp), thiorredoxin glutathione reductase (tgr), and uridine phosphorylase (up) targets were collected from the Protein Data Bank (PDB) database. The docking tests were performed by Autodock Tools (ADT) software version ADT 1.5.6. Subsequently the desloratadine binder was obtained from the PubChem database in 2D structure and designed in the GaussView 5.0 program and optimized by the Gaussian software 09W in the Hartree-Fock method on the Default Spin/3-2G basis. The rest of the parameters were set according to the standard method. Results: Of all the analyzed targets, desloratadine obtained the best results in the up and 2cb1 receptors with binding energies of -8.49 and -8.35 Kcal.mol-1 respectively. Conclusion: These values demonstrate a good molecular affinity in the interaction of the organisms with the drug desloratadine, besides having high results of inhibition constant, demonstrating bioactive activity of the drug antischistosomiasis. With the present in silica results, the drug becomes an alternative in antischistosomiasis bioactive studies, being able to give continuity in vitro and ex vivo assays.