蛋白质分子间相互作用影响土大黄苷-蛋白质组相互作用的研究

The interaction between BLF and BSA and impact in interaction of RT-BSA-BLF system

荧光光谱结合全反射傅立叶红外光谱研究土大黄苷(rhaponticin,RT)与混合蛋白质组[BSA(bovine serum albumin)-BLF(bovine lactoferrin)]的相互作用,分析其相互作用的影响因子。荧光光谱实验表明,药物RT猝灭混合蛋白质组的荧光强度,蛋白质组的最大发射波长明显红移,表明RT与蛋白质组之间存在着相互作用,该相互作用受蛋白质组中单组分蛋白质分子间相互作用及不同组分蛋白质分子间相互作用的影响。本工作建议用总体微环境因子(IOM)来定量表达影响RT-混合蛋白质组之间相互作用的溶液微环境因素。全反射傅立叶红外光谱法实验表明,药物RT与混合蛋白质组的相互作用过程中,蛋白质组中各组分蛋白质分子二级构象均发生了变化,分子结构不同,构象变化程度差异明显。蛋白质组中单组分蛋白质分子间的相互作用影响蛋白质分子二级构象变化,浓度与比例不同,相互作用不同,影响分子构象变化程度不同。荧光光谱与红外光谱结果基本一致,可为研究RT与BSA-BLF蛋白质组相互作用提供探讨性参考。

The binding of rhaponticin to bovine serum albumin（BSA）-bovine lactoferrin（BLF） and the factors that affect BSA-BLF interaction have been studied by fluorescence spectroscopy and Fourier transform infrared spectroscopy. In the fluorescence experiment,RT quenched the fluorescence intensity of mixed proteome and the maximum emission wavelength of BSA,BLF and BSA-BLF proteins system. RT caused obvious red-shift fluorescence for an interaction between RT and proteome. The interaction between RT and proteome was impacted by single-component protein molecular interactions and the interaction between RT-BSA and RT-BLF,the microenvironment of solutions were the factors impacting the interactions between RT and proteome,which impacted quantitative expression of the general environment micro environmental factors. In the Fourier transform infrared spectroscopy,the secondary conformation of protein molecules of single component in the protein group were changed,and the difference of the molecules＇ structure was responsible for the differences in the molecular conformation changes. The molecules＇ interaction in the single-component protein affected secondary conformation of the proteins＇ molecule. The proteins＇ concentration ratio and the interaction were different in degree of molecular conformational change. These data demonstrates an example of combination of fluorescence spectrum experiment with Fourier transform infrared spectroscopy in the study of protein structura.