荧光光谱结合表面增强拉曼光谱法研究紫檀芪与人血清白蛋白相互作用

引用本文: 申炳俊, 金丽虹, 刘昱鑫, 柴浩, 刘占伟, 刘荣娟, 田坚. 荧光光谱结合表面增强拉曼光谱法研究紫檀芪与人血清白蛋白相互作用[J]. 分析化学, 2017, 45(11): 1613-1620. doi: 10.11895/j.issn.0253-3820.170341 shu

Citation: SHEN Bing-Jun, JIN Li-Hong, LIU Yu-Xin, CHAI Hao, LIU Zhan-Wei, LIU Rong-Juan, TIAN Jian. Study of Intermolecular Interactions Between Pterostilbene and Human Serum Albumin by Fluorescence Spectrometry-Surface Enhanced Raman Spectroscopy[J]. Chinese Journal of Analytical Chemistry, 2017, 45(11): 1613-1620. doi: 10.11895/j.issn.0253-3820.170341 shu

荧光光谱结合表面增强拉曼光谱法研究紫檀芪与人血清白蛋白相互作用

申炳俊 ^1, ,
金丽虹 ^2, ,
刘昱鑫 ^2, ,
柴浩 ^2, ,
刘占伟 ^2, ,
刘荣娟 ^2, ,
田坚 ^1,

1.
长春理工大学清洁能源技术研究所, 长春 130022;
2.
长春理工大学生命科学技术学院, 长春 130022
基金项目:
本文系国家自然科学基金（No.21153003）、吉林省教育厅项目（No.201574）和长春理工大学博士后基金项目（2014年）资助

摘要: 在模拟人体生理条件下，应用荧光光谱和表面增强拉曼光谱法研究了紫檀芪（PTE）与人血清白蛋白（HSA）之间相互作用机制。结果表明，HSA的荧光能被PTE静态猝灭，并伴随有非辐射能量转移作用，两者形成了1∶1复合物，结合距离r=1.495 nm，结合常数K_A=1.12×10⁴（298 K）、4.07×10⁴（304 K）和2.45×10⁵ L/mol （310 K）。表面增强拉曼光谱研究揭示，PTE分子通过甲氧基与HSA进行结合；热力学数据表明，二者间的作用主要为疏水作用；标记竞争实验指出PTE优先结合HSA的位点Ⅲ。三维荧光光谱、同步荧光光谱和表面增强拉曼光谱结果显示，与PTE作用后，HSA构象发生变化，导致色氨酸残基周围环境疏水性降低，但对PTE分子构象影响不大。

关键词:

English

Study of Intermolecular Interactions Between Pterostilbene and Human Serum Albumin by Fluorescence Spectrometry-Surface Enhanced Raman Spectroscopy

1.
Laboratory of Clean Energy Technology, Changchun University of Science and Technology, Changchun 130022, China;
2.
School of Life Science and Technology, Changchun University of Science and Technology, Changchun 130022, China
Received Date: 29 May 2017
Revised Date: 19 July 2017
Fund Project:
This work was supported by the National Natural Science Foundation of China (No.21153003).

Abstract: The binding mechanism between pterostilbene (PTE) and human serum albumin (HSA) was investigated by fluorescence spectrometry and surface enhanced Raman spectroscopy (SERS) under simulated physiological conditions. The experiment result showed that the effect between PTE and HSA was a static fluorescence quenching with Förster's non-radioactive energy transformation, and PTE could bind HSA strongly with a 1:1 molar ratio. The binding distances between PTE and HSA was 1.495 nm, and the binding constants (KA) between PTE and HSA were 1.12×10⁴ (298 K), 4.07×10⁴ (304 K) and 2.45×10⁵ L/mol (310 K). SERS revealed that PTE combined with HAS by methoxy group. Thermodynamic data indicated that the interaction between PTE and HSA was mainly hydrophobic interaction. Marker competition experiments pointed out that the primary binding site for PTE was located at site Ⅲ in HSA. Three-dimensional, synchronous fluorescence spectrum and SERS showed that the conformation of HSA changed apparently with the addition of PTE, resulting in the tryptophan residue of HSA exposing to a less hydrophobic micro-environment. However, the conformation of PTE did not change apparently with the addition of HSA.

Key words:

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荧光光谱结合表面增强拉曼光谱法研究紫檀芪与人血清白蛋白相互作用

English

Study of Intermolecular Interactions Between Pterostilbene and Human Serum Albumin by Fluorescence Spectrometry-Surface Enhanced Raman Spectroscopy

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通讯作者: 陈斌, bchen63@163.com

中国化学会秘书处

荧光光谱结合表面增强拉曼光谱法研究紫檀芪与人血清白蛋白相互作用

English

Study of Intermolecular Interactions Between Pterostilbene and Human Serum Albumin by Fluorescence Spectrometry-Surface Enhanced Raman Spectroscopy

CCS Chemistry：嵌段共聚物自组装成 “三明治”二维有机材料，实现纳米级压力传感功能

CCS Chemistry：颜徐州、鲍哲南： 你的皮肤可能是一片SPMs

CCS Chemistry：工作高效不疲劳，只须让催化剂动起来

CCS Chemistry：静电组装导向聚合- 聚电解质纳米凝胶量化制备新策略

CCS Chemistry：金黄色葡萄球菌醛基脱氢酶是如何识别特异性底物的？

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