The Molecular Dynamics and Experimental Verification of the Interaction Between Tannic Acid and Human Serum Albumin Protein
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.
国家科技期刊平台
NSTL
万方数据
