Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design.

To explore the possible binding sites at the interface of tripanosomal triosephosphate isomerase, fully flexible benzothiazoles were docked onto the dimer interface. Docking studies revealed that the most favorable interactions occur in the aromatic clusters of the dimeric form. Hence is purposed that the dimer disruption is not via Cys 15, as presented in last studies, but it could be carried out through the unstabilization of pi-pi interactions of two aromatic clusters present in the interface. These studies enable a novel alternative for rational structure-based anti-tripanosomal drug design.