芦丁与溶菌酶相互作用的光谱研究  

Spectroscopic Studies on the Interaction of Rutin and Lysozyme

作　　者：崔力剑[1] 渠玲玲 杨文月[2] 窦玉红[1] 焦宁[3] 黄芸[2,4] 

机构地区：[1]河北中医学院药学院,河北石家庄050091 [2]河北医科大学药学院,河北石家庄050017 [3]河北医科大学第三医院药剂科,河北石家庄050051 [4]河北医科大学中西医结合研究所,河北石家庄050017

出　　处：《现代食品科技》2014年第6期30-35,共6页Modern Food Science and Technology

基　　金：河北省自然科学基金(08B033);河北省卫生厅重点课题计划(20100241);河北省中医药管理局基金(2012011)

摘　　要：在模拟人体生理pH条件下,采用荧光光谱法和紫外-可见光谱法研究不同温度下(298 K、304 K和310 K)芦丁与溶菌酶相互作用的光谱特征,明确了芦丁对溶菌酶荧光猝灭的机理,确定了二者作用间结合位点及结合常数,测定了芦丁对溶菌酶活性的影响趋势。结果表明芦丁能与溶菌酶发生弱相互作用,该作用是由焓驱动的低温自发反应过程,芦丁通过静态猝灭机制使溶菌酶内源荧光产生猝灭。两者结合位点数接近于1,结合驱动力为氢键或范德华力,298 K时结合距离为4.02 nm。紫外吸收、同步荧光和三维荧光光谱均表明芦丁导致溶菌酶构象变得更加紧密。采用比浊法测定溶菌酶活性结果表明,芦丁可能影响溶菌酶活性位点Asp-52所处微环境极性,不利于Asp-52发挥氢键受体的催化作用,使溶菌酶溶菌活性降低。The interaction of rutin with lysozyme （LYZ） was studied in simulating physiological condition （pH 7.40） at 298 K, 304 K and 310 K by ultraviolet-vis （UV） absorption and fluorescence spectroscopy. The results showed that rutin quenched the endogenous fluorescence of LYZ via a static quenching procedure and the interaction between them was a spontaneous process. The number of binding sites was approximately 1. Van der Waals＇ forces and hydrogen bonds played major roles in stabilizing rutin-LYZ complex, and the distance between the donor and acceptor was 4.02 nm （298 K）. The UV absorption, synchronous fluorescence and three-dimensional fluorescence spectra showed that the conformation of LYZ became more tightly packed. The turbidimetric analysis showed that rutin decreased LYZ activity. Rutin may be bad for the hydrogen-bonding receptor catalysis activity of Asp-52 by affecting the micro-environment of lysozyme activity site （Asp-52）.

关 键 词：芦丁 溶菌酶 静态猝灭 构象 结合常数 活性 

分 类 号：O657.3[理学—分析化学] TS201.25[理学—化学]