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Spectral Studies on the Interaction of Toluidine Blue O with Bovine Serum Albumin

机译:甲苯胺蓝O与牛血清白蛋白相互作用的光谱研究

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摘要

Interaction between toluidine blue O (TBO) and bovine serum albumin (BSA) was investigated by UV-visible absorption and emission spectroscopy. It is proposed that the fluorescence quenching of BSA by TBO was mainly a result of the formation of TBO-BSA complex and electrostatic interactions played an important role to stabilize the complex. The Stern-Volmer quenching constant K_(SV) and corresponding thermodynamic parameters ΔH~0, ΔG~0, and ΔS~0 were evaluated. Results suggest the interaction process to be comparable with the reversible biological processes. Effect of TBO on the conformation of BSA has been analyzed by means of synchronous fluorescence spectroscopy. IR spectra also proved that the interaction of TBO with BSA had changed the conformation of TBO.
机译:通过紫外可见吸收和发射光谱研究了甲苯胺蓝O(TBO)和牛血清白蛋白(BSA)之间的相互作用。有人提出,TBO对BSA的荧光猝灭主要是由于TBO-BSA配合物的形成,静电相互作用对稳定配合物起着重要作用。评价了斯特恩-沃尔默淬灭常数K_(SV)和相应的热力学参数ΔH〜0,ΔG〜0和ΔS〜0。结果表明相互作用过程与可逆的生物过程相当。通过同步荧光光谱法分析了TBO对BSA构象的影响。红外光谱也证明了TBO与BSA的相互作用改变了TBO的构象。

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