引用本文:
曹团武, 杨季冬. 孔雀石绿与牛血清白蛋白的相互作用[J]. 物理化学学报,
2008, 24(04): 715-719.
doi:
10.3866/PKU.WHXB20080430
Citation: CAO Tuan-Wu, YANG Ji-Dong. Interaction between Malachite Green and Bovine Serum Albumin[J]. Acta Physico-Chimica Sinica, 2008, 24(04): 715-719. doi: 10.3866/PKU.WHXB20080430
Citation: CAO Tuan-Wu, YANG Ji-Dong. Interaction between Malachite Green and Bovine Serum Albumin[J]. Acta Physico-Chimica Sinica, 2008, 24(04): 715-719. doi: 10.3866/PKU.WHXB20080430
孔雀石绿与牛血清白蛋白的相互作用
摘要:
运用荧光光谱和紫外-可见吸收光谱研究了在缓冲溶液中不同温度下孔雀石绿(MG)与牛血清白蛋白(BSA)之间的相互作用. 实验结果表明, MG对BSA的内源荧光猝灭为静态猝灭过程. 测定了该反应在不同温度下的结合常数KA, KA分别为7.69×104 L·mol-1(10 ℃)、5.31×104 L·mol-1(20 ℃)和4.85×104 L·mol-1(37 ℃), MG与BSA以摩尔比1:1结合. 根据Forster非辐射能量转移理论, 求出了37 ℃时给体(MG)和受体(BSA)之间能量转移效率和结合距离分别为E=0.1635 和r=2.30 nm. 计算出的热力学参数表明, MG 和BSA之间的作用力主要是通过氢键和范德华力相互作用.
English
Interaction between Malachite Green and Bovine Serum Albumin
Abstract:
The interaction between malachite green (MG) and bovine serum albumin (BSA) was investigated via fluorescence and ultraviolet-visible absorption spectra in buffer solutions at different temperatures. The experimental results showed that static quenching was involved in addingMGin BSAsolution. The binding constants (KA) were 7.69×104 L·mol-1 (10 ℃), 5.31×104 L·mol-1 (20 ℃), and 4.85×104 L·mol-1 (37 ℃), respectively, and they reacted at a molar ratio of 1:1. The energy transfer efficiency E was 0.1635 and the binding distance r was 2.30 nm between MG and BSA according to Forster non-radiative energy transfer mechanism. The interaction between MG and BSA was driven mainly by hydrogen bonds and Vander Waals force according to thermodynamic parameters.
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