单宁酸与人血清白蛋白互作的分子动力学分析和实验验证
The Molecular Dynamics and Experimental Verification of the Interaction Between Tannic Acid and Human Serum Albumin Protein
田鹏 1宋洁 1赵成鹏 1张晨玉 1武棒棒 2赵春贵3
作者信息
- 1. 山西工程科技职业大学 体育学院,山西 太原 030619
- 2. 山西省农业科学院小麦研究所,山西 临汾 041000
- 3. 华侨大学 化工学院,福建 泉州 362021
- 折叠
摘要
本文通过荧光光谱、酶解和分子对接等技术研究了单宁酸(TA)与人血清白蛋白(HSA)之间的仿生作用力和分子动力学模拟.结果表明,TA与HSA的相互作用是一个典型的两阶段反应:快反应阶段(RRS)和慢反应阶段(SRS).在25℃时,结合常数分别为3.16×105 L·mol-1和3.55×108 L·mol-1.荧光光谱表明TA对HSA的猝灭机理是静态猝灭效应,且疏水力在TA与HSA相互作用过程中起着重要作用.基于Förster非辐射能量转移理论,确定TA的结合位点位于亚结构域A的疏水区域,TA与人血清白蛋白Trp212之间的距离分别为2.21 nm(RRS)和1.97 nm(SRS).疏水探针和酶解实验证实TA与HSA之间的相互作用分为两个独立的过程,包括快速反应中的瞬时识别并耦合及慢速反应中的再匹配.本研究验证了TA与HSA的相互作用力,并阐明其反应过程,为植物多酚与蛋白质互作模式的研究提供了参考依据.
Abstract
This study examines the interaction between tannic acid(TA)and human serum albumin(HSA)using fluorescence spec-troscopy,enzymolysis and molecular docking techniques.The results reveal that the interaction process between TA and HSA could be regarded as a typical two-stage reaction:a rapid reaction stage(RRS)and a slow reaction stage(SRS).The binding constants at 25℃are determined to be 3.16×105 L·mol-1 and 3.55×108 L·mol-1,respectively.The analysis of the fluorescence spectra indicates that TA quenches HSA through a static quenching mechanism,with hydrophobic forces playing a significant role in the binding pro-cess.Based on the Förster non-radiative energy transfer theory,the binding site of TA is identified as the hydrophobic region of sub-domain A.The distance between TA and HSA Trp212 are measured to be 2.21 nm in RRS and 1.97 nm in SRS,respectively.Hydro-phobic probe and enzymatic hydrolysis analysis,confirmed that the interaction between TA and HSA was divided into two indepen-dent processes,including instantaneous recognition and coupling in the fast reaction and rematching in the slow reaction.In conclu-sion,this study provides clarification on the interaction mechanism and reaction process between TA and HSA,thereby enhancing our understanding of the interaction between plant polyphenols and proteins.
关键词
快反应/慢反应/荧光光谱/分子对接Key words
rapid reaction/slow reaction/fluorescence spectra/molecular docking引用本文复制引用
基金项目
山西省教育科学"十四五"规划课题(TY-230016)
山西省哲学社会科学项目(2023YJ148)
出版年
2024
国家科技期刊平台
NSTL
万方数据