Interaction between triclosan and bovine hemoglobin
The interaction between triclosan(TCS)and bovine hemoglobin(BHb),a transport protein,was studied at the molecular level by using various spectroscopic methods such as fluorescence spectroscopy,UV visible absorption spectroscopy,circular dichroism,and molecular docking simulation.The experimental results indicate that TCS exhibits a fluorescence quenching effect on BHb,which is caused by the static binding between TCS and BHb.The binding force between TCS and BHb is mainly hydrophobic,and TCS binds with BHb in the ratio of 1∶1.This binding process is spontaneous.TCS affects the microenvironment of amino acids such as tryptophan and tyrosine in BHb,making the overall protein skeleton structure of BHb loose.TCS also affects the secondary protein structure of BHb,leading to an increase in α-helix content and a decrease in β-sheet content.The results of molecular docking simulation indicate that TCS binds to the central hydrophobic cavity of BHb,and there are hydrogen bonds between the TCS and BHb.
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