Exploring the Binding Interaction Mechanism of Taxol in ß-Tubulin and Bovine Serum Albumin: A Biophysical Approach.

In this present study on understanding the taxol (PTX) binding interaction mechanism in both the ß-tubulin and bovine serum albumin (BSA) molecule, various optical spectroscopy and computational techniques were used. The fluorescence steady-state emission spectroscopy result suggests that there is a static quenching mechanism of the PTX drug in both ß-tubulin and BSA, and further time-resolved emission spectroscopy studies confirm that the quenching mechanism exists. The excitation-emission matrix (EEM), Fourier transform infrared, and resonance light scattering spectra (FT-IR) confirm that there are structural changes in both the BSA and ß-tubulin molecule during the binding process of PTX. The molecular docking studies revealed the PTX binding information in BSA, ß-tubulin, and modeled ß-tubulin and the best binding pose to further subject the molecular dynamics simulation, and this study confirms the stability of PTX in the protein complex during the simulation. Density functional theory (DFT) calculations were performed between the free PTX drug and PTX drug (single point) in the protein molecule active site region to understand the internal stability.