【作者】 马纪； 陈鸾； 刘海灵； 谢孟峡；

【Author】 MA Ji,CHEN Luan,LIU Hai-ling,XIE Meng-xia~* Analytical & Testing Center of Beijing Normal University,Beijing 100875,China

【机构】 北京师范大学分析测试中心；

【摘要】 利用荧光、紫外光谱技术研究了3,6-二羟基黄酮（3,6-HF）与人血清白蛋白（HSA）的相互作用,对它们结合机理进行了研究。研究结果表明,在pH值为7.4条件下,3,6-HF对HSA的内源荧光有明显的猝灭现象。3,6-HF可以与HSA发生特异性结合,形成了1:1复合物,结合常数为1.73×10⁵ L·mol^-1,3,6-HF在HSA上只有一个结合位点。紫外光谱显示,在中性和弱碱性条件下,药物的紫外光谱发生明显的红移。3,6-HF与HSA相互作用后,其紫外光谱吸收Ⅰ带发生红移,表明药物与蛋白发生了结合。更多还原

【Abstract】 The interaction of 3,6-dihydroxyflavone(3,6-HF) with human serum albumin(HSA) was studied by UV and fluorescence spectroscopy.Under pH 7.4 conditions,the quenching of HSA intrinsic fluorescence by 3,6-HF was very obvious. Fluorescence spectra results indicated that the presence of one specific binding site on HSA for 3,6-HF,and 3,6-HF had one binding site on HSA,with the binding constant(K_A) of 1.73×10~5 L ? mol~1.There was a significant red shift in the band of UV spectra under neutral and alkalescence conditions.The red shift of UV absorption band I after 3,6-HF interacting with HSA,indicated that 3,6-HF bound to HSA.更多还原