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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 interaction between rhaponticin (RT) and bovine serum albumin (BSA) - BLF (bovine serum albumin) - BLF was studied by fluorescence spectroscopy and total reflection Fourier transform infrared spectroscopy. Fluorescence spectroscopy experiments showed that the fluorescence intensity quenched by RT of the mixture of drugs and the maximum emission wavelength of the proteome significantly red shifted, indicating that there is an interaction between RT and the proteome, which is affected by the single-component protein molecules in the proteome Interactions and Interactions between Different Components of Protein Molecules. This work suggests that total microenvironmental factors (IOMs) are used to quantify the solution microenvironmental factors that affect the interaction between RT-mixed proteomes. Total reflectance Fourier Transform Infrared Spectroscopy (FT-IR) showed that the secondary conformations of the protein molecules in the proteome changed during the interaction between the drug RT and the mixed proteome. The molecular structures were different and the degree of conformational change was significantly different. The interaction between single-component protein molecules in proteome affects the secondary conformational changes of protein molecules, with different concentrations and ratios, different interactions and different degrees of molecular conformational changes. Fluorescence spectra and infrared spectroscopy results are basically the same, can provide a reference for the study RT and BSA-BLF proteome interaction.