光谱法分析苔红素与牛血清白蛋白的相互作用  

Spectral Analysis of the Interaction between Orcein and Bovine Serum Albumin

作　　者：杨莹 胡吉祥 沈毅 王书琴 陈观莹 刘兴艳 徐浩然 童文华 YANG Ying;HU Ji-xiang;SHEN Yi;WANG Shu-qin;CHEN Guan-ying;LIU Xing-yan;XU Hao-ran;TONG Wen-hua(School of Biological Engineering,Sichuan University of Science and Engineering,Yibin 644000,China;Key Laboratory of Brewing Biotechnology and Application,Yibin 644000,China;Sichuan LangJiu Co.Ltd.,Luzhou 646500,China)

机构地区：[1]四川轻化工大学生物工程学院,宜宾644000 [2]酿酒生物技术及应用四川省重点实验室,宜宾644000 [3]四川郎酒股份有限公司,泸州646500

出　　处：《湖南师范大学自然科学学报》2023年第5期145-152,共8页Journal of Natural Science of Hunan Normal University

基　　金：四川省科技厅计划重点研发项目(2022YFS0549);四川省2022年度博士后科研项目特别资助(294074);四川轻化工大学研究生创新基金资助项目(Y2022090);四川轻化工大学大学生创新创业训练计划项目(cx2021143);四川轻化工大学人才引进项目(2019RC31)。

摘　　要：采用荧光、紫外光谱法以及其他多种光谱方法研究苔红素(ORC)与牛血清白蛋白(BSA)的相互作用机理。通过Stern-Volmer原理以及分别计算291,300和309 K温度下的热力学参数,证明ORC与BSA的猝灭方式是联合猝灭;经同步荧光光谱和三维荧光谱分析得出,ORC与BSA的相互作用使BSA的构象发生了明显变化;圆二色谱表明ORC主要与BSA多肽链的氨基酸残基结合;依据分子对接及热力学计算,ORC和BSA之间的主要力是疏水相互作用力。The fluorescence,ultraviolet spectroscopy,and other spectroscopic methods were used to explore the interaction mechanism between orcein(ORC)and bovine serum albumin(BSA).Based on the Stern-Volmer principle and calculations of thermodynamic parameters at 291,300,and 309 K,it can be concluded that the quenching mode of ORC and BSA is the combined quenching.Through the synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy,it is found that the interaction between ORC and BSA alters the conformation of BSA.The circular dichroism chromatography shows that ORC mainly bonds to the amino acid residues of the polypeptide chain in BSA.Molecular docking results show that the main force between ORC and BSA is the hydrophobic interaction force.

关 键 词：苔红素 牛血清白蛋白 荧光光谱 圆二色谱 分子对接 

分 类 号：Q503[生物学—生物化学] O657.3[理学—分析化学]