pH对阿霉素与人血清白蛋白相互作用的影响

Effect of pH on the Interaction of Adriamycin and Human Serum Albumin

应用荧光光谱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F rster理论,求出了5个不同pH下,两者结合的动力学猝灭常数、能量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白的荧光都有猝灭作用;与中性、弱酸和弱碱性环境相比,在pH 4.00的强酸性环境中,两者的猝灭常数明显偏低,结合距离明显偏大.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蛋白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,静电作用不是两者相互作用的主要作用力.

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.