Study of Intermolecular Interactions Between Pterostilbene and Human Serum Albumin by Fluorescence Spectrometry-Surface Enhanced Raman Spectroscopy
10.11895/j.issn.0253-3820.170341
- VernacularTitle: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
- Author:
Jun Bing SHEN
1
;
Hong Li JIN
;
Xin Yu LIU
;
Hao CHAI
;
Wei Zhan LIU
;
Juan Rong LIU
;
Jian TIAN
Author Information
1. 长春理工大学 清洁能源技术研究所
- Keywords:
Pterostilbene;
Human serum albumin;
Fluorescence;
Surface enhanced Raman spectroscopy;
Conformation change
- From:
Chinese Journal of Analytical Chemistry
2017;45(11):1613-1620
- CountryChina
- Language:Chinese
-
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.
