SERS结合光谱法研究正壬酸香草酰胺与人血清白蛋白的相互作用  

Spectroscopic Studies on Interactions Between Human Serum Albumin and Nonivamide

作　　者：周家羽 周光明 陈蓉 罗丹 ZHOU Jia-yu;ZHOU Guang-ming;CHEN Rong;LUO Dan(Key Laboratory of Luminescence and Real-time Analysis of the Ministry of Education,School of Chemistry and Chemical Engineering,Southwest University,Chongqing 400715,China)

机构地区：[1]西南大学化学化工学院,发光与实时分析教育部重点实验室,重庆400715

出　　处：《分析测试学报》2022年第3期361-367,共7页Journal of Instrumental Analysis

基　　金：国家自然科学基金项目(21475014)。

摘　　要：在模拟生理条件下,以金纳米颗粒(AuNPs)作为增强基底,归属正壬酸香草酰胺分子(OC)的表面增强拉曼光谱(SERS)特征峰,确定了其在基底表面的吸附方式。通过对比与人血清白蛋白(HSA)识别前后OC分子SERS光谱的变化情况,推测OC分子通过甲氧基与HSA进行结合,在AuNPs基底上的吸附方式也由垂直吸附转为倾斜吸附。热力学结果显示,氢键、疏水作用力以及范德华力是OC-HSA复合物稳定性的主要推动力。荧光光谱结果揭示,OC分子主要作用于色氨酸残基附近的亚结构域IIA疏水空腔内部,从而使HSA的构象发生变化,导致色氨酸残基周围疏水性升高。这些信息不仅可为研究药物与血浆或血清白蛋白之间相互作用的机理提供参考,还为了解人体中药物的代谢提供了指导。Under simulated physiological conditions, the adsorption mode of nonivamide(OC)on the surface of AuNPs was determined with AuNPs as the Raman substrate.Surface-enhanced Raman spectroscopy(SERS)revealed that the phenolic group of OC combined with human serum albumin(HSA).The influence of HSA on the adsorption mode of OC after recognition was analyzed,and the thermodynamic parameters for the interaction between OC and HSA were calculated.The main binding forces were hydrogen bonds,hydrophobic interaction force and Vander Waals force.and the interaction was strong.The results of fluorescence spectroscopy indicated that OC slightly affected the secondary structure of HSA,and increased the hydrophobicity of the microenvironment around the tryptophan residue.The information could be used not only as a reference for study on the mechanism of interaction between drugs and blood plasma or serum albumin,but also as a guidance to understand the metabolism of drugs in human body.

关 键 词：表面增强拉曼散射(SERS) 荧光光谱 正壬酸香草酰胺 相互作用 人血清白蛋白 

分 类 号：O657.3[理学—分析化学] O629.7[理学—化学]