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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Study on the interaction between Besifloxacin and bovine serum albumin by spectroscopic techniques
Xianyong Yu1, Bingfei Jiang2, Zhixi Liao2
1Key Laboratory of Theoretical Organic Chemistry and Function 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 411201, China; Key Laboratory of Computational Physical Sciences, Fudan University, Ministry of Education, Shanghai, China.
Abstract:
The interaction between Besifloxacin (BFLX) and bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, UV-Vis absorption and circular dichroism) techniques under imitated physiological conditions. The experiments were conducted at different temperatures (298, 304 and 310 K) and the results showed that the BFLX caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant (Ka), binding sites (n) were obtained. The corresponding thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated at different temperatures. The results revealed that the binding process was spontaneous and the acting force between BFLX and BSA were mainly electrostatic forces. According to Förster non-radiation energy transfer theory, the binding distance between BFLX and BSA was calculated to be 4.96 nm. What is more, both synchronous fluorescence and circular dichroism spectra confirmed conformational changes of BSA.
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