谷胱甘肽对丁基化羟基甲苯与牛血清白蛋白作用机制影响的光谱研究  

Spectral Study on the Effect of Glutathione on the Interaction between Butylated Hydroxytoluene and Bovine Serum Albumin

作　　者：吴雨彤 王俊茜 赵刚[1] WU Yu-tong;WANG Jun-qian;ZHAO Gang(College of Chemistry and Materials Engineering,Bohai University,Jinzhou 121013,China)

机构地区：[1]渤海大学化学与材料工程学院,辽宁锦州121013

出　　处：《化学试剂》2024年第8期19-24,共6页Chemical Reagents

基　　金：渤海大学博士启动项目(0522BS028-02/05013)。

摘　　要：丁基化羟基甲苯(BHT)是一种合成酚类抗氧化剂,也是一种潜在的内分泌干扰物。采用荧光光谱法、紫外光谱法和时间分辨荧光光谱法等表征方法,研究了BHT与牛血清白蛋白(BSA)的结合机制,以及谷胱甘肽(GSH)对二者相互作用的影响。BHT主要通过疏水作用与BSA形成较为稳定的复合物(K b=1.11×10^(4) L/mol),并改变了BSA的二级结构。但GSH会改变BHT与BSA的作用力类型,降低BHT与BSA的结合常数(K b=2.11×10^(3) L/mol),抑制BHT与BSA的结合,增大二者的结合距离,并且在一定程度上削弱BHT对BSA二级结构的改变。不过,BHT对1,1-二苯基-2-三硝基苯肼(DPPH自由基)的清除能力不受GSH共存的影响。Butylated hydroxytoluene(BHT)is a synthetic phenolic antioxidant,and also a potential endocrine disruptor.The binding mechanism of BHT to bovine serum albumin(BSA)and the effect of glutathione(GSH)on the interaction were investigated by fluorescence spectroscopy,UV spectroscopy and time-resolved fluorescence spectroscopy.BHT formed stable complex with BSA mainly through hydrophobic interaction(K b=1.11×10^(4) L/mol),and changed the secondary structure of BSA.However,GSH changed the binding forces of BHT and BSA(K b=2.11×10^(3) L/mol),reduced the binding constants,inhibited the binding,increased the binding distance of them,and weakened the changes of BSA secondary structure by BHT in some extent.Fortunately,BHT′s ability to scavenge 2,2-diphenyl-1-pyridine hydrazyl(DPPH)free radicals remained unaffected by GSH coexistence.

关 键 词：丁基化羟基甲苯 牛血清白蛋白 谷胱甘肽 结合机制 光谱法 

分 类 号：O657[理学—分析化学]