食品科学2025，Vol.46Issue(7)：34-42,9.DOI:10.7506/spkx1002-6630-20240612-072
基于荧光光谱法分子动力学模拟探究葛根素与β-乳球蛋白的结合机制
Exploration of the Binding Mechanism between Puerarin and β-Lactoglobulin Using Fluorescence Spectroscopy and Molecular Dynamics Simulation
摘要
Abstract
The binding mechanism of puerarin(PUE)to β-lactoglobulin(β-lg)was investigated by fluorescence spectroscopy,molecular docking,and molecular dynamics simulation.The fluorescence spectroscopy results showed that PUE statically quenched the fluorescence of β-lg.At 25,35,and 45℃,the binding constants were 7.24×104,1.34×105,and 2.18×105 L/mol,and the numbers of binding sites were 1.02,1.18,and 1.15,respectively,indicating there was only one binding site or class of binding sites.Synchronous fluorescence and three-dimensional fluorescence spectroscopy indicated that the binding of PUE to β-lg resulted in an increase in the polarity of the microenvironment of β-lg,thereby weakening the hydrophobic force.Molecular docking results showed that PUE bound to the hydrophobic cavity of β-lg,forming hydrophobic interactions with six amino acid residues of β-lg and short hydrogen bonds with five amino acid residues.The molecular dynamics results showed that the root mean square deviation(RMSD),radius of gyration(Rg),and solvent accessible surface area(SASA)of the complex were(0.17±0.02)nm,(1.47±0.01)nm,and(88.94±2.05)nm2,and those of β-lg were(0.22±0.03)nm,(1.48±0.01)nm,and(90.09±1.73)nm2,respectively.The root mean square fluctuation(RMSF)of the complex was lower than that of β-lg,suggesting that the PUE/β-lg complex has better stability at the molecular level.This study is of reference significance for increasing the bioavailability of PUE.关键词
葛根素/β-乳球蛋白/荧光光谱/分子动力学模拟/非共价相互作用Key words
puerarin/β-lactoglobulin/fluorescence spectroscopy/molecular dynamics simulation/non-covalent interaction分类
轻工业引用本文复制引用
马波,李蓉,徐傲,段文杰,黄业传..基于荧光光谱法分子动力学模拟探究葛根素与β-乳球蛋白的结合机制[J].食品科学,2025,46(7):34-42,9.基金项目
湖北省科技计划项目(2022BEC031) （2022BEC031）
