分析化学2017，Vol.45Issue(11)：1613-1620,8.DOI:10.11895/j.issn.0253-3820.170341
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
Study of Intermolecular Interactions Between Pterostilbene and Human Serum Albumin by Fluorescence Spectrometry-Surface Enhanced Raman Spectroscopy
摘要
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 F?rsterˊ 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.关键词
紫檀芪/人血清白蛋白/荧光光谱/表面增强拉曼光谱/构象变化Key words
Pterostilbene/Human serum albumin/Fluorescence/Surface enhanced Raman spectroscopy/Conformation change引用本文复制引用
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):1613-1620,8.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 This work was supported by the National Natural Science Foundation of China (No. 21153003). （No. 21153003）
