黄芩与牛血清白蛋白相互作用的光谱特性研究OA

To investigate the interaction mechanism of scutellaria baicalensis georgi(SBG)produced in Daqing with bovine serum albumin(BSA),the aqueous extract of SBG was used as the material.The interaction mechanism,main binding forces,thermodynamic parameters,and binding sites were determined by fluorescence spectroscopy.The results showed that the fluorescence intensity of BSA was regularly quenched with the increase of SBG aqueous extract concentration,and the fluorescence peak exhibited a red shift of 6 nm,indicating the occurrence of binding and enhanced polarity of the microenvironment around tryptophan residues.Based on the binding number less than one and the thermodynamic parameters(△H>0,and △S>0,△G<0),it was concluded that SBG showed weak binding ability to BSA,and the interaction was driven mainly by hydrophobic forces.Synchronous fluorescence spectroscopy further revealed that the polarity of the tryptophan microenvironment was increased and hydrophobicity was decreased,while the conformation tyrosine residues was not significantly changed,suggesting that the interaction primarily occurred near tryptophan residues.This study helps clarify the binding mechanism of SBG with BSA and provides theoretical and experimental data for understanding the behavior of SBG in blood circulation.