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Interaction between fasudil hydrochloride and bovine serum albumin: spectroscopic study |
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| Authors: | Xianyong Yu Bingfei Jiang Caifang Xun Qing Yao |
| Institution: | 1. Key Laboratory of Theoretical Organic Chemistry and Functional Molecule, Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, China;2. Key Laboratory of Computational Physical Sciences, Fudan University, Ministry of Education, Shanghai, People's Republic of China |
| Abstract: | The interaction between fasudil hydrochloride (FSD) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy under imitated physiological conditions. The Stern–Volmer quenching model has been successfully applied and the results revealed that FSD could quench the intrinsic fluorescence of BSA effectively via static quenching. The binding constants and binding sites for the BSA–FSD system were evaluated. The corresponding thermodynamic parameters obtained at different temperatures indicated that hydrophobic force played a major role in the interaction of FSD and BSA. The distance between the donor (BSA) and the acceptor (FSD) was obtained according to fluorescence resonance energy transfer (FRET). Synchronous fluorescence spectroscopy and FT‐IR spectra showed that the conformation of BSA was changed in the presence of FSD. Copyright © 2015 John Wiley & Sons, Ltd. |
| Keywords: | fasudil hydrochloride bovine serum albumin fluorescence spectroscopy ultraviolet spectroscopy interaction |