Department of Physics, School of Physics and Information Engineering, Fuzhou University, Fuzhou 350108, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Oct;96:132-8. doi: 10.1016/j.saa.2012.05.013. Epub 2012 May 14.
The interaction between pyrrolizine derivatives (PD) and bovine serum albumin (BSA) under imitated physiological conditions was analyzed by fluorescence and ultraviolet spectra. The experiments were conducted at three different temperatures (302, 306 and 310 K) and the results showed that PD caused the fluorescence quenching of BSA through a combined quenching procedure. The binding constant (K(a)), binding-site number (n) between PD and BSA at different temperatures were obtained. According to Förster non-radiation energy transfer theory, the binding distance (r) between BSA and PD was calculated. The corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) were also obtained. The comparison of binding potency of PD and BSA suggested that the substituent on the benzene ring could enhance the binding affinity of PD and BSA. Finally, we investigated the possible sub-domain on BSA where bind PD by displacement experiments.
在模拟生理条件下，通过荧光和紫外光谱分析了吡咯里嗪衍生物 (PD) 与牛血清白蛋白 (BSA) 之间的相互作用。实验在三个不同温度（302、306 和 310 K）下进行，结果表明 PD 通过联合猝灭过程引起 BSA 的荧光猝灭。获得了 PD 与 BSA 在不同温度下的结合常数 (K(a)) 和结合位点数 (n)。根据福斯特非辐射能量转移理论，计算了 BSA 与 PD 之间的结合距离 (r)。还获得了相应的热力学参数 (ΔG、ΔH 和 ΔS)。PD 和 BSA 结合能力的比较表明，苯环上的取代基可以增强 PD 与 BSA 的结合亲和力。最后，我们通过置换实验研究了 PD 可能结合的 BSA 上的可能亚域。
