摘要
在模拟人体生理条件下,利用分子对接模拟、三维荧光光谱、内源荧光光谱和同步荧光光谱,研究了保泰松(PBZ)与人血清白蛋白(HSA)间作用机理。三维荧光和同步荧光光谱表明,PBZ使HSA微环境和构象发生改变。荧光光谱结果表明,PBZ通过静态与非辐射能量转移联合猝灭HSA内源荧光,两者间结合常数为1.96×10^(4) L/mol(310 K),结合距离为0.65 nm。范特霍夫定律计算得到的热力学参数(ΔH=-58.88 kJ/mol和ΔS=54.68 J/(mol·K))说明,PBZ与HSA之间的主要作用力为疏水作用力。分子对接结果显示,PBZ通过疏水作用力与HSA的亚域ⅡA中氨基酸残基进行作用,PBZ周围4.0Å区域还存在ⅠB、ⅡB、ⅢA亚结构域的17个氨基酸残基。本研究有助于从分子水平了解PBZ在人体内的储藏运输过程以及对蛋白质功能的影响机制。
Under the condition of simulating human physiology,the action between Phenylbutazone(PBZ)and human serum albumin(HSA)is studied by using molecular simulation,three-dimensional fluorescence spectra,fluorescence spectra and synchronous fluorescence spectra.Three-dimensional fluorescence and synchronous fluorescence analysis shows that the presence of PBZ reduces HSA fluorescence intensity and changes the HSA micro-environment and composition.Fluorescence spectra show that PBZ can effectively annihilate HSA endofly fluorescence,and the annihilation mechanism is static annihilation and non-radiation energy transfer.The Lineweaver-Burk equation is combined with a constant of 1.96×104 L/mol(310 K),the binding distance r is 0.65 nm.The thermodynamic parameters calculated by Van’t Hoff’s law(ΔH=58.88 kJ/mol andΔS=54.68 J/(mol·K)),indicating that the main force between PBZ and HSA is hydrophobic.Molecular docking results show that WF functions with amino acid residues in HSA’s sub-domain IIA by hydrophobic force,and there are still 17 amino acid residues in the 4.0 area around PBZⅠB,ⅡB,andⅢA substructification domains.
作者
侯利杰
张泽
申炳俊
金丽虹
HOU Lijie;ZHANG Ze;SHEN Bingjun;JIN Lihong(School of Life Science and Technology,Changchun University of Science and Technology,Changchun 130022)
出处
《长春理工大学学报（自然科学版）》
2021年第6期131-137,共7页
Journal of Changchun University of Science and Technology(Natural Science Edition)
基金
吉林省科技厅发展计划项目(20191102011YY)
长春理工大学科技创新基金(JJLG-2018-14)。
关键词
保泰松
人血清白蛋白
分子对接
荧光光谱
相互作用
Phenylbutazone
human serum albumin
molecular docking simulation
fluorescence spectrum
interaction
