Tubulin is a potent molecular target for development of anticancer agents. In this report, the
binding of non-steroidal anti-inflammatory drugs as tubulin inhibitors potential are investigated by
extensive computational techniques, such as, molecular docking, molecular dynamics simulations and
binding free energy calculations. The results suggest that a potent indomethacin derivative inhibits the
tubulin polymerization by interacting on the colchicine-site binding. This potential chemotherapeutic
agent showed high stability in the molecular dynamics simulations, when complexed on the same
binding site of colchicine, a potent and toxic, tubulin inhibitor. Then, our results can be useful designing new compounds
for cancer treatments.