Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study.
Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study.
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DOI：
10.1016/j.jpha.2016.05.009
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发表时间：
2017-03
影响因子：
8.8
通讯作者：
Das TK
中科院分区：
文献类型：
--
作者：
Roy S;Nandi RK;Ganai S;Majumdar KC;Das TK
用多光谱技术研究了含磷杂环化合物与牛血清白蛋白（BSA）的相互作用。结果表明，PHs对BSA具有很高的结合亲和力，因为它能猝灭BSA的内源荧光。实验结果表明，PHs与BSA之间的荧光猝灭机制为动态猝灭。紫外-可见光谱研究表明，PH-1、PH-2和PH-3与BSA的表观缔合常数Kapp分别为9.25×102、1.27×104和9.01×102 L/mol。根据Förster的非辐射能量转移（FRET）理论，计算了BSA与PHs的结合距离。PH-1、PH-2和PH-3的结合距离（r）分别为2.86、3.03和5.12 nm，表明PH与BSA之间发生了能量转移。由荧光猝灭数据得到的PHs的结合常数随温度的升高而降低。热力学参数ΔH、ΔS和ΔG在不同温度下均为负值，说明该结合过程是自发的，氢键和货车范德华相互作用是稳定复合物的主要作用力。用同步荧光和圆二色性（CD）技术研究了蛋白结合位点的微环境，结果表明PHs的存在改变了BSA的构象。最后，我们利用Autodock研究了BSA与PHs的对接，结果表明，PHs位于BSA结构域之间的裂缝中。光谱法研究了BSA与PHs的相互作用。荧光猝灭机制是动态的。货车范德华力和氢键是BSA与PHs相互作用的主要作用力。PHs-BSA相互作用的对接。
Interaction between bovine serum albumin (BSA) and phosphorus heterocycles (PHs) was studied using multi-spectroscopic techniques. The results indicated the high binding affinity of PHs to BSA as it quenches the intrinsic fluorescence of BSA. The experimental data suggested the fluorescence quenching mechanism between PHs and BSA as a dynamic quenching. From the UV–vis studies, the apparent association constant (Kapp) was found to be 9.25×102, 1.27×104 and 9.01×102 L/mol for the interaction of BSA with PH-1, PH-2 and PH-3 respectively. According to the Förster's non-radiation energy transfer (FRET) theory, the binding distances between BSA and PHs were calculated. The binding distances (r) of PH-1, PH-2 and PH-3 were found to be 2.86, 3.03, and 5.12 nm, respectively, indicating energy transfer occurs between BSA and PHs. The binding constants of the PHs obtained from the fluorescence quenching data were found to be decreased with increase of temperature. The negative values of the thermodynamic parameters ΔH, ΔS and ΔG at different temperatures revealed that the binding process is spontaneous; hydrogen bonds and van der Waals interaction were the main force to stabilize the complex. The microenvironment of the protein-binding site was studied by synchronous fluorescence and circular dichroism (CD) techniques and data indicated that the conformation of BSA changed in the presence of PHs. Finally, we studied the BSA-PHs docking using Autodock and results suggest that PHs is located in the cleft between the domains of BSA. The interaction between BSA and PHs by spectroscopic methods. The fluorescence quenching mechanism is dynamic. Van der Waals force and hydrogen bond are the main force for BSA-PHs interaction. Docking of PHs-BSA interaction.
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影响因子：
3.8
作者：
Hu, YJ;Liu, Y;Qu, SS
通讯作者：
Qu, SS
DOI：
10.1016/j.jpba.2005.01.023
发表时间：
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