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 π-π interactions of two aromatic clusters present in the interface. These studies enable a novel alternative for rational structure-based anti-tripanosomal drug design.
Bibliographical noteFunding Information:
We thank Drs. Armando Gómez-Puyou, Ruy Pérez-Montfort and Arturo Rojo-Dominguez for fruitful discussions about this work. This work was supported under CONACYT and CGPI-IPN grants 31935 and 200860.