光谱学与光谱分析
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应用荧光猝灭法研究尼莫地平与牛血清白蛋白的相互作用
吴秋华,王春,王志* ,宋双居
河北农业大学理学院,河北 保定 071001
Study on the Interaction of Nimodipine and Bovine Serum Albumin by Fluorescence Quenching Method
WU Qiu-hua,WANG Chun,WANG Zhi* ,SONG Shuang-ju
College of Science, Agricultural University of Hebei, Baoding 071001, China
摘要 : 应用荧光光谱(FS)和紫外光谱(UV)研究了尼莫地平与牛血清白蛋白(BSA)之间的相互作用。尼莫地平与BSA的结合常数K A 为5.01×104 (26 ℃)和4.46×104 (36 ℃),尼莫地平在BSA上的结合位点数为1.08±0.01。根据Frster非辐射能量转移理论,求出了尼莫地平与BSA之间的结合距离为3.14 nm(26 ℃)和3.10 nm(36 ℃)。实验表明静态猝灭和非辐射能量转移是 导致尼莫地平对BSA荧光猝灭的两大原因。通过计算热力学参数,可知该药物与牛血清白蛋白的相互作用是一个吉布斯自由能降低的自发过程,且二者之间的作用力以静电相互作用为主。
关键词 :荧光光谱法;尼莫地平;牛血清白蛋白;相互作用
Abstract :The interaction of Nimodipine and bovine serum albumin (BSA) was studied using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The apparent binding constants (K A ) between Nimodipine and BSA were 5.01×104 (26 ℃) and 4.46×104 (36 ℃), and the binding sites (n) were 1.08±0.01. According to the Frster theory of non-radiation energy transfer, the binding distances (r) were also obtained. The experimental results showed that Nimodipine could quench the inner fluorescence of BSA by forming the Nimodipine-BSA complex. It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching. The process of binding was a spontaneous molecular interaction in which entropy increased while Gibbs free energy decreased. The thermodynamic parameters indicated that the interaction of Nimodipoine and BSA was driven mainly by static electrical force.
Key words :Fluorescence spectroscopy;Nimodipine;Bovine serum albumin;Interaction
收稿日期: 2006-06-21
修订日期: 2006-09-25
通讯作者:
王志
E-mail: wangzhi@mail.hebau.edu.cn
引用本文:
吴秋华,王春,王志* ,宋双居. 应用荧光猝灭法研究尼莫地平与牛血清白蛋白的相互作用[J]. 光谱学与光谱分析, 2007, 27(11): 2317-2320.
WU Qiu-hua,WANG Chun,WANG Zhi* ,SONG Shuang-ju. Study on the Interaction of Nimodipine and Bovine Serum Albumin by Fluorescence Quenching Method. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(11): 2317-2320.
链接本文:
https://www.gpxygpfx.com/CN/Y2007/V27/I11/2317
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