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pH对阿霉素与人血清白蛋白相互作用的影响
引用本文:林爱华,冯艾荣,汤凯,胡兴,邹国林. pH对阿霉素与人血清白蛋白相互作用的影响[J]. 武汉大学学报(理学版), 2005, 51(6): 749-752
作者姓名:林爱华  冯艾荣  汤凯  胡兴  邹国林
作者单位:武汉大学,生命科学学院,湖北,武汉,430072
基金项目:国家自然科学基金资助项目(30370366),教育部高等学校博士学科点专项研究基金资助项目
摘    要:应用荧光光潜的方法研究了阿霉素与人血清白蛋白的相互作用.基于荧光猝灭现象和Firster理论,求出了5个不同pH下,两者结合的动力学猝火常数、能节转移效率和结合距离等参数.发现:在实验的酸度条件下,阿霉素对人血清白蛋门的荧光都有猝火作用;与中性、弱酸和弱碱性环境相比,存pH4.00的强酸性环境中,两者的猝灭常数明显偏低,结合距离叫显偏大.结果表明:阿霉素与人血清白蛋白的结合过程中,非辐射能量转移是导致人血清白蟹自荧光猝灭的原因之一;中性、弱酸和弱碱性环境对两者的结合不会产生太大的影响,静电作用小早两者相互作用的主要作用力。

关 键 词:阿霉素  人血清白蛋门  非辐射能鞋转移  荧光猝灭
文章编号:1671-8836(2005)06-0749-04
修稿时间:2005-04-25

Effect of pH on the Interaction of Adriamycin and Human Serum Albumin
LIN Ai-hua,FENG Ai-rong,TANG Kai,HU Xing,ZOU Guo-lin. Effect of pH on the Interaction of Adriamycin and Human Serum Albumin[J]. JOurnal of Wuhan University:Natural Science Edition, 2005, 51(6): 749-752
Authors:LIN Ai-hua  FENG Ai-rong  TANG Kai  HU Xing  ZOU Guo-lin
Abstract:The interaction of Adriamycin with Human Serum Albumin was studied by fluorescence spectroscopy.Based on the fluorescence quenching of human serum albumin and F rster energy transfer mechanism,Stern-Volmer quenching constants,energy transfer efficiencies and the binding distances of Trp-214 residue to the binding site of Adriamycin were estimated under five different pH.The results showed that Adriamycin has an ability to quench human serum albumin fluorescence and compared with under other pH conditions,the Stern-Volmer quenching constants was lower and the binding distance was larger under pH 4.00. Non-radiative energy transfer was the reason of fluorescence quenching.It was not obviously observed influence on the binding of adriamycin and human serum albumin under neutral pH,subacidity and alkalescent conditions,electrostatic interaction was not the main binding force.
Keywords:adriamycin  human serum albumin  non-radiative energy transfer  fluorescence quenching
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