期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 255, 期 -, 页码 -出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2021.119662
关键词
4-Octylphenol; Human serum albumin; Spectrophotometry; Molecular docking; Molecular dynamics simulation
类别
资金
- National Natural Science Foundation of China [22078143]
- Jiangxi Provincial Natural Science Foundation [20202BAB205005]
- Research Program of State Key Laboratory of Food Science and Technology Nanchang University [SKLF-ZZB-201914, SKLF-ZZA-201912]
4-Octylphenol interacts with human serum albumin to form a ground state complex governed by hydrogen bonds and hydrophobic forces, affecting the structure and properties of HSA.
4-Octylphenol (OP) is an environmental estrogen that can enter organisms through the food chain and cause various toxic effects. Here, the interaction between OP and human serum albumin (HSA) was explored through multipectral, molecular docking and dynamics simulation. The results showed that OP and HSA formed a ground state complex through a static quenching mechanism, and the interaction was spontaneously driven by hydrogen bonds and hydrophobic interaction forces. The binding constant at different temperatures was measured to be on the order of 10(5) L mol(-1). Site competition experiments suggested that OP interacted with amino acid residues Lys195, Cy245 and Cys246 located at the Sudlow site I of HSA, resulting in a more stretched protein peptide. The presence of OP increased the surface hydrophobicity of HSA, and reduced the content of a-helix in HSA by 3.4%. FT-IR spectra showed that OP interacted with the C=O and C-H groups of the polypeptide backbone. Molecular docking demonstrated that OP mainly bound to Site I of HSA and hydrogen bonds participated in the interaction. In addition, molecular dynamics simulations further explored the stability and dynamic behavior of the OP-HSA complex through RMSD, RMSF, SASA and Rg. (C) 2021 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据