The interaction of imPeratorin and isoimPeratorin with HSA in the Presence of metal Ions
TONG Yue-ju
HAO Juan
FU ZhenG-qinG
WANG Juan
HAN DonG
ZHANG Ai-pinG
Abstract：Objective To obtain the intensity of fluorescence quenching,binding — site number,binding constant,the influence of reaction type and its effect on the space conformation under simulated human physiological conditions. Methods The interaction of imperatorin and isoimperatorin with human serum albumin(HSA)were investigated using the fluores-cence spectroscopy and synchronous fluorescence spectroscopy in the presence of metal ions. Results Imperatorin and iso-imperatorin enhanced the fluorescence quenching of HSA in the presence of metal ions,as well as conjugation. The hydrogen bond and vander waals force were the major driving force between the imperatorin,imperatorin and HSA. Their strength of force was changed,but the type of driving force unchanged in the presence of different metal ions. For the imperatorin,the order of force strength was Mg2 + > Cu2 + > Ni2 + > Co2 + > Zn2 + > Fe3 + > Al3 + ,for isoimperatorin,the order was Cu2 + >Zn2 + > Fe3 + > Co2 + > Mg2 + > Al3 + > Ni2 + . The results of synchronous fluorescence spectroscopy indicated that the confor-mation of HSA was changed by imperatorin or isoimperatorin in the presence of metal ions. Conclusion The presence of metal ions promoted the imperatorin and isoimperatorin interact with human serum albumin.
Keywords：Metal ionsHuman serum albuminImperatorinIsoimperatorinFluorescence spectroscopySynchronous fluorescence spectroscopy
Publication Date：2015-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：5( 132-136 )