鹅膏蕈氨酸与人血清蛋白相互作用机制的研究  

Study on the mechanism of interaction between ibotenic acid and human serum albumin

作　　者：张孟丽 陈慧慧 郑世杰 吴芳芳 谭栀恩 张蕊 ZHANG Meng-li;CHEN Hui-hui;ZHENG Shi-jie;WU Fang-fang;TAN Zhi-en;ZHANG Rui(National Engineering Laboratory for the Development of Southwestern Endangered Medicinal Materials, Guangxi Botanical Garden of Medicinal Plant,Nanning 530023,China;Shandong Key Lab of Edible Mushroom Technology,Ludong University,Yantai 264025,China;CECEP GUANGXI Clean Tech Development Company Ltd.Nanning 530024,China)

机构地区：[1]广西壮族自治区药用植物园西南濒危药材资源开发国家工程实验室,广西壮族自治区南宁530023 [2]鲁东大学农学院,山东烟台264025 [3]中节能(广西)清洁技术发展有限公司,广西壮族自治区南宁530024

出　　处：《化学研究与应用》2021年第11期2222-2227,共6页Chemical Research and Application

基　　金：国家自然科学基金项目(31200048)资助;烟台市重点研发计划项目(2019XDHZ092)资助。

摘　　要：在模拟生理条件下,采用荧光光谱分析鹅膏蕈氨酸(Ibotenic acid,IBO)与人血清蛋白(Human serum albumin,HSA)相互作用的猝灭机制、结合常数和结合位点数,根据热力学方程计算热力学参数和作用力类型。采用同步荧光光谱和三维荧光光谱分析相互作用过程中的构象变化。结果表明:IBO通过静态和动态相结合的猝灭机制猝灭人血清白蛋白的内源荧光。温度对结合过程影响比较大。结合过程轻微地改变人血清白蛋白的结构和微环境。范德华力和氢键是结合过程中的主要作用力。Under simulated physiological conditions,fluorescence spectroscopy was used to analyze the quenching mechanism,binding constant and number of binding sites of the interaction between ibotenic acid(IBO)and human serum albumin(HSA),and calculated according to the thermodynamic equation thermodynamic parameters and type of force.Synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy were used to analyze the conformational changes during the interaction.The results show that:IBO quenches the endogenous fluorescence of human serum albumin through a combination of static and dynamic quenching mechanisms.Temperature has a greater influence on the bonding process.The binding process slightly changes the structure and microenvironment of human serum albumin.Van der Waals forces and hydrogen bonds are the main forces in the bonding process.

关 键 词：鹅膏蕈氨酸 人血清蛋白 荧光光谱 内源性荧光 相互作用 

分 类 号：O629[理学—有机化学]