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一种八极化合物的合成及其对血清白蛋白的生物学效应。

Synthesis of an octupolar compound and its biological effects on serum albumin.

作者信息

Zhang Hua-xin, Gao Song, Yang Xi-xiong

机构信息

College of Chemical and Pharmaceutical Engineering, Jingchu University of Technology, Jingmen, Hubei, 448000, People's Republic of China.

出版信息

Mol Biol Rep. 2009 Jul;36(6):1405-11. doi: 10.1007/s11033-008-9329-x. Epub 2008 Aug 14.

Abstract

A special rigid planar structural octupolar molecule titled 2,4,6-tris(p-methylstyryl)-s-triazine (TMT) was synthesized and its interaction with bovine serum albumin (BSA) were studied by molecular spectroscopy. The quenching mechanism of fluorescence of BSA by TMT was discussed. The thermodynamic parameters DeltaH(theta), DeltaG(theta), DeltaS(theta) at different temperatures were calculated and the results indicate hydrogen bond forces played major role in the reaction and the reaction was mainly enthalpy-driven. The distance r between donor (BSA) and acceptor (TMT) was obtained according to Förster theory of non-radiation energy transfer. Circular dichroism (CD) spectra, synchronous and three-dimensional fluorescence spectra were used to investigate the structural change of BSA molecules with addition of TMT, the result indicates that the alpha-helical structures of BSA molecules reduced in the presence of TMT. Sketch map of the interaction process was analyzed at molecular level.

摘要

合成了一种名为2,4,6-三(对甲基苯乙烯基)-均三嗪(TMT)的特殊刚性平面结构八极分子,并通过分子光谱研究了其与牛血清白蛋白(BSA)的相互作用。探讨了TMT对BSA荧光的猝灭机制。计算了不同温度下的热力学参数ΔH(θ)、ΔG(θ)、ΔS(θ),结果表明氢键力在反应中起主要作用,且反应主要由焓驱动。根据Förster非辐射能量转移理论得到了供体(BSA)与受体(TMT)之间的距离r。利用圆二色性(CD)光谱、同步荧光光谱和三维荧光光谱研究了添加TMT后BSA分子的结构变化,结果表明在TMT存在下BSA分子的α-螺旋结构减少。在分子水平上分析了相互作用过程的示意图。

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