盐酸萘甲唑啉与牛血清白蛋白相互作用的光谱分析。
Spectroscopic analyses on interaction of Naphazoline hydrochloride with bovine serum albumin.
机构信息
Farming Development Services Center, Jinghai, 300016 Tianjin, China.
出版信息
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Dec;98:142-7. doi: 10.1016/j.saa.2012.08.040. Epub 2012 Aug 23.
The fluorescence and ultraviolet spectroscopy were explored to study the interaction between Naphazoline hydrochloride (Naphcon) and bovine serum albumin (BSA) at three different temperatures (292, 301, and 310 K) under imitated physiological conditions. The quenching mechanism of BSA by Naphacon was interpreted using the Stern-Volmer mechanism, and a combined quenching (dynamic and static quenching). The binding constants, binding sites and the corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) of the interaction system were calculated at different temperatures. According to Förster non-radiation energy transfer theory, the binding distance between BSA and Naphcon was found to be 4.71 nm. Synchronous fluorescence spectroscopy showed the conformation of BSA changed in the presence of Naphacon. In addition, the effect of some common metal ions (Mg(2+), Ca(2+), Ni(2+), Cu(2+), and Fe(2+)) on the binding constant between Naphcon and BSA was examined.
采用荧光光谱法和紫外光谱法，在模拟生理条件下，于三个不同温度（292、301 和 310 K）下研究了盐酸萘甲唑啉（萘甲唑林）与牛血清白蛋白（BSA）之间的相互作用。用 Stern-Volmer 机制解释了 BSA 被萘甲唑啉猝灭的机制，并进行了复合猝灭（动态猝灭和静态猝灭）。在不同温度下计算了相互作用体系的结合常数、结合位点数和相应的热力学参数（ΔG、ΔH 和 ΔS）。根据 Förster 非辐射能量转移理论，发现 BSA 与萘甲唑啉之间的结合距离为 4.71nm。同步荧光光谱表明，在存在萘甲唑啉的情况下，BSA 的构象发生了变化。此外，还考察了一些常见金属离子（Mg(2+)、Ca(2+)、Ni(2+)、Cu(2+)和 Fe(2+)）对萘甲唑啉与 BSA 之间结合常数的影响。
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