Molecular Docking and Spectroscopic Exploring of the Binding Intermolecular between BSA with Complex of Zirconium

Abstract

In this study, the mechanism of the binding interaction of Zr(CUR), a novel six-coordinate complex of zirconium with a curcumin ligand and bovine serum albumin (BSA), was elucidated via fluorescence spectroscopy, Fourier transform infrared spectroscopy and molecular modeling methods. The analysis indicated that Zr(CUR) could effectively quench the endogenous fluorescence of BSA, forming a 1 : 1 complex with a static quenching mechanism. The distance between the donor (BSA) and acceptor [Zr(CUR)] was determined to be 1.19 nm on the basis of Forester’s theory of nonradiative energy transfer. The results of the infrared absorption spectrum revealed that the secondary structure of BSA changed. The molecular docking results demonstrated that the Zr(CUR) with the minimum binding energy is at position IIIA. Furthermore, as shown by the docking study, Zr(CUR) has several hydrogen bonds and van der Waals contacts with BSA. The synchronous fluorescence and Fourier transform infrared spectroscopy data revealed that Zr(CUR) could lead to conformational changes in BSA, which could affect its biological functions.