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首页> 外文期刊>New Journal of Chemistry >Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique
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Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique

机译：光谱技术研究地塞米松磷酸钠与牛血清白蛋白的相互作用特性

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摘要

The interaction of dexamethasone sodium phosphate (DEX-P) with bovine serum albumin (BSA) was studied by fluorescence quenching in combination with UV-Vis spectroscopic method under near physiological conditions. Fluorescence quenching rate constants and binding constants for BSA-DEX-P system were determined at different temperatures. The fluorescence quenching of BSA by DEX-P was due to static quenching and energy transfer. The results of thermodynamic parameters, AH (-161.0 kJ mol~(-1)), AS (-468.0 J mol~(-1) K~(-1)) and AG (-21.54 to -16.86 kJ mol~(-1)}, indicated that van der Waals interaction and hydrogen bonding played a major role in DEX-P-BSA association. Competitive experiments demonstrated that the primary binding site of DEX-P on BSA was located at site III in sub-domain lll_A of BSA. The distance between BSA and DEX-P was estimated to be 1.23 nm based on the Forster resonance energy transfer theory. The binding constant (K_a) of BSA-DEX-P at 298 K was 2.239 x 10~4 L mol~(-1) Circular dichroism spectra, synchronous fluorescence and three-dimensional fluorescence studies showed that the presence of DEX-P could change the conformation of BSA during the binding process.
机译：通过荧光猝灭结合紫外可见光谱法研究了地塞米松磷酸钠（DEX-P）与牛血清白蛋白（BSA）的相互作用。在不同温度下测定BSA-DEX-P系统的荧光猝灭速率常数和结合常数。 DEX-P对BSA的荧光猝灭是由于静态猝灭和能量转移。热力学参数AH（-161.0 kJ mol〜（-1）），AS（-468.0 J mol〜（-1）K〜（-1））和AG（-21.54至-16.86 kJ mol〜（-） 1）}，表明范德华相互作用和氢键在DEX-P-BSA缔合中起主要作用，竞争实验表明，DEX-P在BSA上的主要结合位点位于BSA子域III_A的III位。根据福斯特共振能量转移理论，BSA与DEX-P的距离为1.23 nm，BSA-DEX-P在298 K的结合常数（K_a）为2.239 x 10〜4 L mol〜（ -1）圆二色性光谱，同步荧光和三维荧光研究表明，DEX-P的存在可以改变结合过程中BSA的构象。

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