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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 21-(Ph-NN)-NCTPP 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 21-(Ph-NN)-NCTPP and bovine serum albumin (BSA) was investigated by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy under imitated physiological conditions. The results showed that the intrinsic fluorescence of BSA was quenched strongly by 21-(Ph-NN)-NCTPP. The binding constants (Ka) and the binding sites (n) were obtained at three different temperatures (298, 304, and 310K). The thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated, the results indicated that the binding process was spontaneous and the hydrophobic interaction played a major role in [21-(Ph-NN)-NCTPP]-BSA binding process. Based on the Förster non-radiation energy transfer theory, the binding distance from 21-(Ph-NN)-NCTPP to BSA was estimated to be about 3.51nm. What's more, the synchronous fluorescence spectra indicated that the conformation of BSA has not been changed.
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