荧光光谱法研究刺槐素与BSA的相互作用

目的：研究刺槐素（ACA）与牛血清白蛋白（BSA）相互作用的光谱学特性;方法：在模拟人体生理条件下（pH=7.4）,应用荧光光谱法和紫外光谱法研究ACA与BSA的结合作用;结果：ACA可以通过静态猝灭使得BSA荧光强度减弱;在298 K下,ACA与BSA结合常数为1.13×105L/mol,结合位点数为1.011;结合距离为4.45 nm;ACA与BSA作用力主要为氢键和范德华力;ACA与BSA的同步荧光光谱表明,ACA与BSA的结合对蛋白质的构象未产生影响,其结合位点更接近于色氨酸;结论：ACA与BSA存在较强的结合作用,人体内必须的金属离子对ACA与BSA结合能力具有一定的影响。

Study of the Interaction between Acacetin and Bovine Serum Albumin by Fluorescence Spectroscopy

Objective： To study of the binding interaction between acacetin（ACA） and bovine serum albumin（BSA）;Methods： fluorescence spectroscopy and UV-vis spectroscopy were used to research the binding interaction between ACA and BSA under the simulative physiological conditions（pH=7.4）.Results： ACA can give rise to the fluorescence quenching of BSA through static quenching procedure.The binding constants（kA） and the number of binding sites（n） were calculated to be 1.13 × 105 L mol-1 and 1.011,the binding distances was determined to be about 4.45 nm based on Frster nonradiative energy theory,at 298 K.Hydrogen bonds and Van der Waals forces played a major role in the binding of ACA to BSA.The binding interaction between BSA and ACA did not change the conformation of BSA and the binding sites of ACA to BSA were near tryptophan residues via synchronous fluorescence spectrometry;Conclusion： The ACA had a strong binding interaction with BSA;which was influenced by some metal ions exist in the body.