ABSTRACT
In the present study, the interaction between Perfluorohexadecanoic acid (PFHxDA) and human serum albumin (HAS) was studied by fluorescence spectroscopy, molecular docking, dynamic simulation and circular dichroism (CD). The interaction character and the effect on human serum albumin conformation were measured by simulating the physiological condition (pH= 7.4). Experiments and simulation results revealed that PFHxDA molecules and HSA have regular fluorescence quenching, and the quenching mechanism is static quenching and non-radiative energy transfer. Thermodynamic analysis revealed the binding behavior was mainly governed by hydrophobic forces. Specific binding site experiments showed that the binding site of PFHxDA was a site I of HSA. The results from the CD spectrum demonstrated that PFHxDA changed the molecular conformation of HSA, which is consistent with the results obtained by molecular docking and dynamic simulation.