锌离子对灯盏花素与溶菌酶相互作用的影响  

Effect of Zinc Iron on Interaction between Breviscapine and Lysozyme

作　　者：郑茂东[1] 颜娟[1] 王爱萍[1] 赵秀花[1] 徐今宁[1] 

机构地区：[1]河北北方学院附属第一医院,河北张家口075000

出　　处：《中国药业》2016年第4期24-26,共3页China Pharmaceuticals

基　　金：河北省自然科学基金资助项目;项目编号:H4014405031;河北省卫生厅资助项目;项目编号:ZD20140167;河北省张家口市科技局资助项目;项目编号:1421132D

摘　　要：目的在模拟人体生理条件下,研究Zn^(2+)对灯盏花素与溶菌酶相互作用的影响。方法采用紫外光谱法、荧光光谱法研究Zn^(2+)对灯盏花素与溶菌酶相互作用机制、作用力类型的影响。结果有无Zn^(2+)存在,灯盏花素与溶菌酶的荧光猝灭机制均为静态猝灭和非辐射能量转移;灯盏花素与溶菌酶的结合常数(K)分别为1.24×10~6 L/mol和1.08×10~6 L/mol,结合位点数(n)分别为1.05和1.19,结合距离(r)分别为1.96 nm和2.05 nm,其作用力均以疏水作用为主。结论Zn^(2+)不改变灯盏花素与溶菌酶的作用机制,但能使两者结合的结合常数、结合距离、结合位点数发生改变。Objective To study the effect of Zn^2＋ on the interaction between breviscapme and lysozyme under the simulative human physiological condition.Methods The interaction between breviscapme with lysozyme,with or without Zn^2＋ was investigated using ultraviolet spectroscopy and fluorescence spectroscopy.Results The results of fluorescence spectrometry showed that the endogenous fluorescence of lysozyme had been significantly quenched by breviscapine of fluorescence quenching were static quenching with non-radiation energy transfer.The binding parameters of breviscapine and lysozyme were as follows：with or without Zn^2＋,the binding constants K were1.24×10^6 L/mol,1.08×10^6 L/mol,the numbers of binding site were 1.05,1.19,binding distances were 1.96 nm,2.05 nm respectively.And the major driving force was hydrophobic force.Conclusion The results shows that the presence of Zn^2＋ does not affect the quenching mechanism,but changes the binding constants,the numbers of binding site and the binding distances.

关 键 词：锌离子 灯盏花素 溶菌酶 荧光光谱法 

分 类 号：R285.5[医药卫生—中药学] R282.71[医药卫生—中医学]