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作 者:赵晓飞[1] 徐靖源[1] 谢承志[1] 欧阳燕[1]
机构地区:[1]天津医科大学药学院天津市临床药物关键技术重点实验室,天津300070
出 处:《天津医科大学学报》2013年第4期279-281,共3页Journal of Tianjin Medical University
基 金:国家自然科学基金面上项目(20971099)
摘 要:目的:研究铜配合物与人血清蛋白(HSA)的相互作用,为了更深入了解金属药物在体内发挥作用的机制。方法:利用荧光光谱法,探讨两个多吡啶铜配合物对HSA的荧光猝灭机制,以及与HSA结合位点个数和作用方式。结果:配合物1和2的荧光猝灭机制均为动态猝灭。两个配合物与HSA的结合位点个数为1,通过热力学参数推断出两个配合物与HSA之间主要靠疏水作用力结合。同步荧光色谱指出两个配合物影响了HSA中色氨酸的周围环境。结论:两个铜配合物能够与HSA有很好的结合能力,为成为药物提供了可能性,也为进一步开发和研究两个铜配合物的生物活性提供了可能的途径和依据。Objective: To study the interaction between copper complex and human bovine serum (HSA) to know the mechanism of metal complex in vivo. Methods: The study discussed the fluorescence quenching mechanism, the number of binding sites and the mode of action of two polypyridyl copper complexes to HSA by fluorescence spectrometry. Results: The research results showed that the fluorescence quenching of HSA by complexes 1 and 2 was induced by a dynamic quenching mechanism. The number of binding to HSA was close to one for both complexes, which bound to HSA through hydrophobic interactions and influenced the tryptophan residues. Conclusion: The two copper complexes exhibit high binding activity to HSA. The results show that two copper complexes have the potential ability to become drugs, and they also provide a possible way to further explore the biological activities of the two complexes.
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