Title
Comprehensive Insights into Interaction Mechanism between Perfluorodecanoic Acid and Human Serum Albumin.
Author
Sichen Gao, Rutao Liu
Year
2018
Journal
New Journal of Chemistry
Abstract
This investigation explored toxic mechanism of perfluorodecanoic acid (PFDA) on human serum albumin (HSA), established interaction mode of PFDA with HSA and provided a new strategy for the toxicity evaluation of PFDA on functional protein. The binding of PFDA and HSA forms a complex and PFDA induces the fluorescence sensitization of HSA. Meanwhile, PFDA gives rise to a slight impact on the polypeptide chain and the microenvironment around Trp-214 from the spectroscopic angle. Moreover, the relative esterase activity of HSA depressed by more than 60% upon 4 × 10-4 M PFDA. The thermodynamic parameters ΔG, ΔH and ΔS were -7.2683 kcal∙mol-1, -2.718 × 104 0.5308 × 104 cal∙mol-1 and -66.8 cal∙mol-1∙K-1, which evidenced a spontaneous interaction in which Van der Waals' force and intermolecular hydrogen bond are the predominant driven force. In addition, molecular simulation was applied to determine the specific binding site, which revealed PFDA most preferably binds with Tyr-411 by hydrogen bond and the distance between hydroxyl of PFDA and Tyr-411 is 2.64 Å, in accordance with the conclusion of thermodynamic analysis and HSA functional analysis.
Instrument
J-810
Keywords
Circular dichroism, Secondary structure, Ligand binding, Biochemistry