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光谱分析法研究八羧酸酞菁铝配合物与牛血清白蛋白的结合作用
引用本文:陈奎治,彭亦如,林伟,曹育红,徐国兴,翁家宝.光谱分析法研究八羧酸酞菁铝配合物与牛血清白蛋白的结合作用[J].光谱学与光谱分析,2007,27(1):84-87.
作者姓名:陈奎治  彭亦如  林伟  曹育红  徐国兴  翁家宝
作者单位:1. 福建师范大学化学与材料学院,福建,福州,350007
2. 福建医科大学附属第一医院,福建,福州,350004
3. 福建师范大学化学与材料学院,福建,福州,350007;中国科学院福建物质结构研究所结构化学国家重点实验室,福建,福州,350003
基金项目:福建省自然科学基金 , 福建省青年科技人才创新基金 , 福建省教育厅科研项目 , 国家重点实验室基金 , 国家自然科学基金 , 教育部科学技术研究项目
摘    要:以八羧酸酞菁铝配合物(AlPc(COOH)8)为红区荧光探针,用紫外光谱和荧光光谱分析方法研究了(AlPc(COOH)8)与牛血清白蛋白(BSA)的结合作用,测定了八羧酸酞菁铝与牛血清白蛋白(BSA)的结合位置数和结合常数,结果分别为n=5.7,K=5.74×105和K=3.51×105,两种分析方法结果基本一致.以氯血红素(HE)、布洛芬(IB)、L-色氨酸(TRP)为分子探针,用络合竞争法研究了它们对AlPc(COOH)8-BSA体系紫外光谱的影响,结果表明,往体系中加入HE后,AlPc(COOH)8的单体吸收峰增强,体系由结合态往游离态"转变",而加入TRP和IB后,吸收光谱未观察到明显的变化,由此确定AlPc(COOH)8与BSA的结合点为SiteⅠ.

关 键 词:八羧酸酞菁铝  牛血清白蛋白  竞争络合  结合常数
文章编号:1000-0593(2007)01-0084-04
收稿时间:2005-12-16
修稿时间:2006-03-26

Synthesis and Characterization of Octa-Carboxylic Phthalocyanine Aluminum and Its Interaction with Bovine Serum Albumin
CHEN Kui-zhi,PENG Yi-ru,LIN Wei,CAO Yu-hong,XU Guo-xing,WENG Jia-bao.Synthesis and Characterization of Octa-Carboxylic Phthalocyanine Aluminum and Its Interaction with Bovine Serum Albumin[J].Spectroscopy and Spectral Analysis,2007,27(1):84-87.
Authors:CHEN Kui-zhi  PENG Yi-ru  LIN Wei  CAO Yu-hong  XU Guo-xing  WENG Jia-bao
Institution:1. College of Chemistry and Materials, Fujian Normal University, Fuzhou 350007, China ;2. The First Affiliated Hospital of Fujian Medical University, Fuzhou 350004, China; 3. State Key Laboratory for Structure Chemistry, Chinese Academy of Sciences, Fuzhou 350003, China
Abstract:Octa-carboxylic phthalocyanine aluminium (AlPc(COOH)8) was used as fluorescent probe of infrared region. The interaction of octa-carboxylic phthalocyanine aluminium (AlPc(COOH)s) and bovine serum albumin(BSA) was studied by UV/ Vis and fluorescence spectra methods. The binding constant KA and n of phthalocyanine aluminium with BSA were determined. The results were K=5. 74 X 10(5) , n= 5. 7 and K= 3. 51 X 10(5) , for these two methods respectively. The same results by using two different analytical methods were obtained. Besides, hemin chloride(HE), ibuprofen(IB) and L-tryptophan(TRP) were used as probes, and the effects of these probes on the spectra of AlPc(COOH)8 )-BSA were studied by competitive binding method. The result indicated that, by adding HE into the AlPc(COOH)8)-BSA system, obvious spectral change of the system was observed, while adding TRP and IB caused no spectral changes. The binding site of octa-carboxylic phthalocyanine aluminium on the BSA was found to be at the I site by competitive binding method.
Keywords:Octa-carboxylic phthalocyanine aluminium  Bovine serum albumin  Competitive complexation  Binding constant
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