Study on the interaction between benzocaine and bovine serum albumin with fluorescence spectroscopy
Author(s): XIANG Canhui, WANG Wenjun, GUO Danni, ZHONG Dongmei, TIAN Liang, Department of Bioengineering, Zhuhai Campus of Zunyi Medical University
Pages: 527-532
Year: 2016 Issue: 4
Journal: Journal of Natural Science of Heilongjiang University
Keyword: benzocaine; bovine serum albumin; fluorescence spectroscopy; synchronous fluorescence spectroscopy;
Abstract: The interaction between benzocaine（ BZC） and bovine serum albumin（ BSA） was investigated by fluorescence and ultraviolet-visible spectroscopy. The number of binding sites n（ 0. 87） and binding constant( K4 a,1. 11 × 10L·mol-1) were calculated through fluorescence quenching method,which indicates that the molar ratio of BSA to BZC in complex is about 1 ∶ 1. The biological macromolecule quenching constants（ kq） were measured to be 1. 52 × 1012 L · mol-1·s-1（ p H 7. 4,291 K） and1. 39 × 1012L·mol-1·s-1（ p H 7. 4,310 K）,respectively. The results indicated that the combination reaction between BZC and BSA was a static quenching process. And,the change of the conformation of BSA was also studied by synchronous fluorescence spectroscopy,the results showed that the presence of BZC didn’t affect the microenvironment around the tyrosine and tryptophan residues.
Pages: 527-532
Year: 2016 Issue: 4
Journal: Journal of Natural Science of Heilongjiang University
Keyword: benzocaine; bovine serum albumin; fluorescence spectroscopy; synchronous fluorescence spectroscopy;
Abstract: The interaction between benzocaine（ BZC） and bovine serum albumin（ BSA） was investigated by fluorescence and ultraviolet-visible spectroscopy. The number of binding sites n（ 0. 87） and binding constant( K4 a,1. 11 × 10L·mol-1) were calculated through fluorescence quenching method,which indicates that the molar ratio of BSA to BZC in complex is about 1 ∶ 1. The biological macromolecule quenching constants（ kq） were measured to be 1. 52 × 1012 L · mol-1·s-1（ p H 7. 4,291 K） and1. 39 × 1012L·mol-1·s-1（ p H 7. 4,310 K）,respectively. The results indicated that the combination reaction between BZC and BSA was a static quenching process. And,the change of the conformation of BSA was also studied by synchronous fluorescence spectroscopy,the results showed that the presence of BZC didn’t affect the microenvironment around the tyrosine and tryptophan residues.
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