光谱法研究石墨烯-TiO_2与溶菌酶的相互作用及对酶活性的影响  

Study on Interaction of GR-TiO_2 with Lysozyme and Its Influence on Enzyme Activity by Spectroscopy

作　　者：付正卿 仝月菊[1] 王玲[1] 梁红丽[1] 李莎[1] 张爱平[1] 

机构地区：[1]山西医科大学药学院,山西太原030001

出　　处：《分析测试学报》2015年第9期1027-1033,共7页Journal of Instrumental Analysis

基　　金：山西省自然科学基金资助项目(2010011048-1);山西省自然科学基金(2015011012);山西医科大学科技创新基金资助项目(01200806);山西医科大学博士启动基金(2005204)

摘　　要：在模拟人体生理条件下,采用紫外光谱、荧光光谱、同步荧光光谱、三维荧光光谱和圆二色谱等方法,以纳米Ti O2作对照,研究GR-Ti O2与溶菌酶(LYSO)的相互作用,通过酶活性实验测定GR-Ti O2对LYSO活性的影响。荧光光谱结果表明GR-Ti O2与LYSO发生了相互作用,导致LYSO内源荧光猝灭,猝灭机制为静态猝灭,作用力类型为氢键和范德华力,与纳米Ti O2研究结果一致。同步荧光与圆二色谱结果进一步表明GR-Ti O2对LYSO的构象影响更大。酶活性实验结果表明GR-Ti O2对LYSO的活性抑制作用强于纳米Ti O2。Under the simulative human physiological conditions,using nano-Ti O2 as the control,the interaction of GR- Ti O2 with lysozyme（ LYSO） was investigated by ultraviolet spectrometry,fluorescence spectroscopy,synchronous fluorescence spectroscopy,three-dimensional fluorescence spectroscopy and circular dichroism. The enzyme activity was determined in the presence of GR- Ti O2. The results of fluorescence spectroscopy revealed that the endogenous fluorescence of LYSO was quenched by GR- Ti O2 and its mechanism was static quenching. The major driving forces were hydrogen bonds and van der Waals＇ forces. These results of GR- Ti O2 were consistent with that of nano-Ti O2. The results of synchronous fluorescence and circular dichroism spectra further demonstrated that the conformation of LYSO influenced by GR- Ti O2 was more than that by nano Ti O2. The result of enzyme activity indicated that the enzyme activity of LYSO was inhibited more strongly by GR- Ti O2.

关 键 词：石墨烯-TiO2 纳米TIO2 溶菌酶 光谱法 酶活性 

分 类 号：O657.3[理学—分析化学] O629.8[理学—化学]