化学
等温滴定量热法
氢键
范德瓦尔斯力
牛血清白蛋白
猝灭(荧光)
疏水效应
滴定法
结合常数
荧光
色谱法
结合位点
分子
无机化学
有机化学
物理化学
生物化学
量子力学
物理
作者
Wenjie Liang,Zhenxuan Zhang,Qingyao Zhu,Zekun Han,Chen Huang,Xiong Liu,Mengting Yang
标识
DOI:10.1016/j.saa.2022.122054
摘要
The issue of disinfection byproducts (DBPs) in the water has received critical attention due to the health effects on humans. In the water environment, interactions between bovine serum albumins (BSA), the most abundant water-soluble protein, and DBPs unavoidably occur. In this study, comparative binding interactions of two aromatic DBPs - 2,4,6-trichlorophenol (TCP) and 2,4,6-tribromophenol (TBP) with BSA were investigated systematically utilizing fluorescence spectrometry, UV absorption spectrometry, isothermal titration calorimetry and molecular docking approach. The fluorescence quenching results indicated that TCP/TBP could quench the endogenous fluorescence of BSA through static quenching mechanisms, and TBP showed a more substantial quenching effect. The binding constants were determined for TCP-BSA (3.638 × 105 L/mol, 303 K) and TBP-BSA (6.394 × 105 L/mol, 303 K) complexes, with TBP showing higher binding affinity than TCP. The thermodynamic study and docking analysis suggested that hydrogen bonding and van der Waals forces were the primary interaction forces. Both of TCP and TBP were located in the subdomain IIIA of BSA, and TBP could form more stable complex than TCP. The results of the present study contributed valuable information on the environmental behaviors of halophenols in water environment from perspectives of binding with BSA.
科研通智能强力驱动
Strongly Powered by AbleSci AI