Effect of acidity on the interaction of Oflxacin and bovine serum albumin

被引：0

作者：

Tang, Zhen-Qiang ^{[1
,2
]}

He, Gan-Wu ^{[3
]}

Yi, Ping-Gui ^{[1
,2
]}

机构：

[1] School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China

[2] Molecular Structure-Activity Relationship Key Lab., Hunan Province University, Xiangtan 411201, China

[3] Shaoyang University, Shaoyang 422004, China

来源：

Guang Pu Xue Yu Guang Pu Fen Xi/Spectroscopy and Spectral Analysis | 2008年 / 28卷 / 05期

关键词：

Acidity - Drug interactions - Electrostatics - Energy transfer - Fluorescence spectroscopy - pH - Quenching;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

Bovine serum albumin (BSA) exists as N (pH-7.0), B (pH-9.0), and E (pH 5 L&middotmo&middotl-1, binding distance of r = 2.55 nm and quenching efficiency of 8.63 × 104 L&middotmo&middotl-1 at pH 4.9. Non-radiative energy transfer and static quenching were the cause of fluorescence quenching. The influence on the binding of Oflxacin and bovine serum albumin under neutral, subacidity and alkalescent conditions was not obviously observed, and the electrostatic interaction was not the main force. The effect of Oflx on the conformation of BSA was also investigated using synchronous fluorescence spectrometry.

引用

页码：1107 / 1110