Department of Chemistry, Zhengzhou University, Zhengzhou 450001, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Oct;96:324-31. doi: 10.1016/j.saa.2012.05.030. Epub 2012 May 26.
This work was designed to study the interaction between bovine serum albumin (BSA) and Biphenyldicarboxylate (DDB) or analogs (I, II and III) of DDB by UV-visible and fluorescence spectroscopic methods for the first time. Results showed that both DDB and analogs had a strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constants (K) were calculated according to the relevant fluorescence data. The thermodynamic parameters (ΔH, ΔS and ΔG) showed that the hydrophobic force played a major role in the binding interaction between BSA and DDB or analogs. Synchronous fluorescence spectra of BSA were investigated in the presence of DDB or analogs. It was showed that DDB was the strongest quencher and bound to BSA with the highest affinity among four compounds. The influence of molecular structure on the binding aspects was reported.
本工作首次采用紫外-可见分光光度法和荧光光谱法研究了牛血清白蛋白（BSA）与联苯二甲酸（DDB）或 DDB 的类似物（I、II 和 III）之间的相互作用。结果表明，DDB 和类似物均通过静态猝灭过程具有很强的猝灭 BSA 内源性荧光的能力。根据相关荧光数据计算了结合常数（K）。热力学参数（ΔH、ΔS 和 ΔG）表明，疏水作用力在 BSA 与 DDB 或类似物之间的结合相互作用中起主要作用。在存在 DDB 或类似物的情况下研究了 BSA 的同步荧光光谱。结果表明，DDB 是最强的猝灭剂，在这四种化合物中与 BSA 具有最高的亲和力。报道了分子结构对结合方面的影响。
