Study of conformational and functional changes caused by binding of environmental pollutant tonalide to human serum albumin

人血清白蛋白 化学 圆二色性 生物物理学 疏水效应 对接(动物) 分子动力学 猝灭(荧光) 荧光光谱法 亲脂性 荧光 色氨酸 结合位点 立体化学 生物化学 计算化学 氨基酸 生物 医学 物理 量子力学 护理部
作者
Hongzhao Xiang,Qiaomei Sun,Wenjing Wang,Shixin Liu,Xi Xiang,Zhiqiang Li,Xiaoxiang Liao,Hui Li
出处
期刊:Chemosphere [Elsevier]
卷期号:270: 129431-129431 被引量:30
标识
DOI:10.1016/j.chemosphere.2020.129431
摘要

Tonalide (AHTN) is a new category of pollutants with a wide range of potential environmental and organismal hazards due to its persistence and lipophilicity, and the safety evaluation of this pollutant under physiological condition is a pressing issue. This study investigated the mechanism of interaction between AHTN and human serum albumin (HSA) that is an important transporter in plasma using multiple spectroscopic, molecular docking, and dynamics simulation methods. The steady-state fluorescence and fluorescence lifetime experiments showed that AHTN quenches the inherent fluorescence of HSA through a static quenching mechanism. Thermodynamic parameters exhibited that the binding constant of AHTN and HSA is of the order of 10^4 L/mol, and the binding is a spontaneous process of moderate strength with hydrophobic forces as the main driving force. Site competition revealed that AHTN binds to site I of HSA IIA subdomain, which was evidenced by the molecular docking results. AHTN altered the HSA amino acid microenvironment and conformation can be derived from three-dimensional fluorescence, circular dichroism spectroscopy, and molecular dynamics simulation. The computer simulations corroborate the experimental results positively. Moreover, AHTN acted as a competitive inhibitor to weaken the esterase-like activity of HSA, leading to impaired function of HSA. Results suggest that interactions between AHTN and HSA may affect the normal structure and activities of the protein, this insight will be helpful to provide some basic information to further explore the potential hazards of AHTN in humans.
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