期刊
BMC CHEMISTRY
卷 13, 期 -, 页码 -出版社
BMC
DOI: 10.1186/s13065-019-0615-6
关键词
Sodium benzoate; Bovine serum albumin; Multi-spectroscopy; Molecular docking modeling
资金
- National Natural Science Foundation of China [11474363, 11672339]
- Guangdong Natural Science Funds [2015A030313082]
- Guangzhou science and technology key project [201707020002]
Sodium benzoate (SB) is widely used as a preservative in food industry, and bovine serum albumin (BSA) is a major carrier protein similar to human serum albumin (HSA), the study of the binding between the two has great significance on human health. In this paper, we systematically investigated the binding of SB and BSA under the simulated physiological conditions combining with various common analytical methods, e.g., fluorescence, UV-vis absorption, synchronous fluorescence and circular dichroism (CD) spectra, as well as molecular docking method. The fluorescence quenching measurements were respectively carried out at 298 K, 303 K and 308 K using the Stern-Volmer method. The results reveal that ground state SB-BSA complex was formed within the binding constants from 2.02 x 10(4) to 7.9 x 10(3) M-1. Meanwhile, the negative values of Delta H-0 (-43.92 kJ mol(-1)) and Delta S-0 (- 111.6 J mol(-1) K-1) demonstrated that both the hydrogen binding interaction and van der Waals forces contributed to stabilizing the SB-BSA complex. The site marker competitive experiments show that the SB and BSA bound at site I. Furthermore, the experimental results of UV-vis absorption, synchronous fluorescence and CD spectra indicate that the binding of SB and BSA may change the conformation of BSA. In addition, the molecular docking experiment suggests that hydrogen bond was formed in the interaction between SB and BSA.
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