化学学报 ›› 2011, Vol. 69 ›› Issue (03): 298-304. 上一篇    下一篇

研究论文

纳米氧化钛与小鼠乙酰胆碱酯酶的作用关系

赵海泉*,1,洪法水2   

  1. (1安徽农业大学生命科学学院 合肥 230036)
    (2苏州大学医学部 苏州 215123)
  • 投稿日期:2010-04-09 修回日期:2010-08-03 发布日期:2010-10-09
  • 通讯作者: 赵海泉 E-mail:swjs12@ahau.edu.cn
  • 基金资助:

    纳米氧化钛对小鼠肝功能破坏的分子机制

Interaction between Titanium Dioxide Nanoparticles and Acetylcholin Esterase of Mice

Zhao Haiquan*,1 Hong Fashui2   

  1. (1 College of Life Sciences, Anhui Agriculture University, Hefei 230036)
    (2 Medical College, Soochow University, Suzhou 215123)
  • Received:2010-04-09 Revised:2010-08-03 Published:2010-10-09
  • Contact: Haiquan Zhao E-mail:swjs12@ahau.edu.cn
  • Supported by:

    Molecular mechanisms of nano-dioxide titanium on the liver function damage of mice

纳米TiO2已在各领域得到广泛应用, 由于其小尺寸效应、表面效应、量子尺寸效应等性质因而具有很强的生物学效应, 易进入人体内, 因而担心对人的健康构成潜在危害作用, 但其作用机制不明朗. 通过体内和体外实验相结合的研究方法, 运用光谱学的手段, 研究了纳米TiO2颗粒与乙酰胆碱酯酶(AChE)结构-功能的作用关系. 结果表明, 在体内, 随着纳米TiO2颗粒处理剂量的增加, AChE活性明显增加. 在体外, 一定浓度范围内纳米TiO2颗粒对AChE有显著的激活作用. 光谱学分析证实纳米TiO2颗粒与AChE直接发生结合作用, 强结合位点数为1.6个, 结合常数为2.56×107 L•mol-1, 而弱结合位点的结合常数为3.06×106 L•mol-1. 过多纳米TiO2颗粒的结合将导致AChE去折叠并破坏其二级结构. 提示纳米TiO2颗粒处理引起小鼠体内AChE活性的变化可能与纳米TiO2颗粒结合后引起AChE的结构变化有密切关系.

关键词: 纳米氧化钛, 小鼠, 乙酰胆碱酯酶, 光谱特征, 结构-功能

TiO2 nanoparticles have increasingly been used in the various fields. However, it is these unique characteristics such as small sizes, large surface per mass, and high reactivity that TiO2 nanoparticles can enter the human body quickly and then imposes potential risks on human health. In order to study the mechanisms underlying the effects of TiO2 nanoparticles on acetylcholine esterase (AChE, EC3.1.1.7) of mice, ICR mices were injected with TiO2 nanoparticles (5 nm) of various doses into the abdominal cavity daily for 14 d. We then examined AChE activity in vivo and in vitro and directly evident for interaction between TiO2 nanoparticles and AChE using spectral methods. The results showed that TiO2 nanoparticles could significantly activate AChE in vivo and in vitro. By spectral assays, the TiO2 nanoparticles were determined to be directly bound to AChE, AChE had 1.6 strong binding sites for TiO2 nanoparticles, and their binding constants of the binding sites were 2.56×107 L•mol-1, while the binding constants were 3.06×106 L•mol-1 for the weak binding sites. And TiO2 nanoparticles induced the protein unfolding and secondary structure damage of AChE. It was concluded that the binding of TiO2 nanoparticles altered AChe structure and function.

Key words: titanium dioxide nanoparticle, mice, acetylcholine esterase, spectral characteristics, structure-function