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Comparative Study on the Interaction Between Bovine Serum Albumin and Different Chlorophenols by Spectroscopic Approach

机译:光谱法研究牛血清白蛋白与不同氯酚相互作用的比较

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摘要

The interaction of 4-chlorophenol (4-CP), 2,4-dichlorophenol (2,4-DCP) and pentachlorophenol (PCP), with bovine serum albumin (BSA) was investigated by means of fluorescence spectrometry under simulative physiological conditions. It was found that the intrinsic fluorescence of BSA was quenched uniformly at low PCP concentration or higher 2,4-DCP concentration, while the fluorescence quench of BSA was not observed with the addition of 4-CP. The fluorescence data analysis indicated that PCP and 2,4-DCP bind strongly to BSA by complex formation and the association constants determined by static quenching equation were calculated to be 3.44 x 10~3 and 1.82 x 10~4 L mol~(-1) at 298 K for PCP-BSA and 2,4-DCP-BSA interaction, respeetively. The binding affinity order of the three chlorophenols is PCP > 2,4-DCP > 4-CP. The thermodynamic calculation implied that hydrophobic interaction and electrostatic interaction involved in the interaction process. Conformation investigation results confirmed BSA is predominantlyα-helical although the microenvironment of BSA was partly changed with the addition of PCP or 2,4-DCP.
机译:在模拟生理条件下,通过荧光光谱法研究了4-氯苯酚(4-CP),2,4-二氯苯酚(2,4-DCP)和五氯苯酚(PCP)与牛血清白蛋白(BSA)的相互作用。发现在低PCP浓度或较高的2,4-DCP浓度下,BSA的固有荧光被均匀淬灭,而在添加4-CP时未观察到BSA的荧光淬灭。荧光数据分析表明,PCP和2,4-DCP通过复合物形成与BSA牢固结合,通过静态猝灭方程确定的缔合常数分别为3.44 x 10〜3和1.82 x 10〜4 L mol〜(-1) )在298 K时重复进行PCP-BSA和2,4-DCP-BSA相互作用。三种氯酚的结合亲和力顺序为PCP> 2,4-DCP> 4-CP。热力学计算表明相互作用过程涉及疏水相互作用和静电相互作用。构象研究结果证实,尽管添加PCP或2,4-DCP可以部分改变BSA的微环境,但BSA主要是α-螺旋。

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