In the first part of this work, the interactions of three Schiff bases with human serum albumin (HSA) have been investigated by different kinds of molecular modeling and spectroscopic techniques. Molecular docking study indicated that all Schiff bases bind to the subdomain IB of HSA. Molecular dynamics results suggested that all Schiff bases can interact with HSA, without affecting the secondary structure of HSA but probably with a slight modification of its tertiary structure. Furthermore, the experimental data suggested that all Schiff bases demonstrated a significant binding affinity to HSA and the process is enthalpy driven. In the second part, docking tools were utilized in order to design of novel ??-Tubulin Inhibitors. For this purpose, more than one hundred derivatives of TPS-A were designed and the interactions of them with ??-tubulin were analyzed. Thirteen designed analogous among them as the best docked compounds were selected on the basis of binding energy. Moreover, docking tools were utilized in order to study the binding properties of a series of proline-based 2, 5- diketopiperazine (about 500compounds) in the binding site of ??-tubulin. Results revealed the stronger anti-tubulin activity of twenty compounds among them in comparison with tryprostatin-A, as a well known tubulin inhibitor.
