荧光光谱法研究健那绿B与牛血清白蛋白的相互作用

• 作 者: 王迎进 郭敏敏 孔丽霞 闫军 张海容
• 机 构: 忻州师范学院生化分析技术研究所,
• 出 处: 中国卫生检验杂志
• 发表日期: 2013年03期
• 关键词: 健那绿 荧光光谱 紫外光谱 血清白蛋白 位点数 静态猝灭 结合常数 荧光猝灭 猝灭常数 色氨酸残基

目的:研究健那绿B与牛血清白蛋白(BSA)之间的相互作用。方法:在模拟生理条件下,应用荧光光谱和紫外光谱法测定健那绿B与BSA的结合平衡常数Kb、结合位点数n,结合距离r及其热力学函数ΔH、ΔS、ΔG。结果:健那绿B与BSA在300 K,305 K和310 K时结合常数分别为1.5410×106,1.4077×106和1.3709×106L/mol,结合位点数n近似为1,结合距离r为1.55 nm。结论:健那绿B对BSA的荧光猝灭机制是以静态猝灭为主,二者之间作用力主要是静电引力。健那绿B的介入对BSA的构象影响较小。

Objective: To study the interaction between Kinabalin B and bovine serum albumin (BSA). METHODS: Under simulated physiological conditions, the binding constant Kb, the number of binding sites n, the binding distance r and the thermodynamic functions ΔH, ΔS, ΔG were determined by fluorescence spectroscopy and UV spectrophotometry. Results: The binding constants of Kinabalin B and BSA were 1.5410 × 106, 1.4077 × 106 and 1.3709 × 106L / mol respectively at 300 K, 305 K and 310 K, the number of binding sites n was approximately 1, and the binding distance r was 1.55 nm . Conclusion: The fluorescence quenching mechanism of Kinabalu B to BSA is mainly static quenching, and the interaction force between the two is mainly electrostatic attraction. Kinabalone B intervention on the conformation of BSA less.