Docking simulation between HIV peptidase inhibitors and Trypanosoma cruzi aspartyl peptidase.
Vanessa V S CastilhoKeyla C S GonçalvesKarina M RebelloLuiz P R BaptistaLeandro S SangenitoHelena L C SantosMarta H BranquinhaAndré L S SantosRubem F S Menna-BarretoAna C GuimarãesClaudia Masini d'Avila-LevyPublished in: BMC research notes (2018)
The 3D structure confirmed the presence of acid aspartic residues, which are critical to enzyme activity. The docking experiment revealed that HIV IPs bind to the active site of the enzyme, being ritonavir and lopinavir the ones with greater affinity. Benznidazole presented the worst binding affinity, this drug is currently used in Chagas' disease treatment and was included as negative control. These results together with previous data on the trypanocidal effect of the HIV PIs support the hypothesis that a T. cruzi aspartyl peptidase can be the intracellular target of these inhibitors. However, the direct demonstration of the inhibition of T. cruzi aspartyl peptidase activity by HIV PIs is still a goal to be persuaded.