新型尾式卟啉的合成及与人血清白蛋白的相互作用  

Synthesis of New Tailed Porphyrins and Studies on the Interaction Between Metalloporphyrins and HSA

作　　者：彭玉苓[1] 王树军[1] 郭玉明[1] 

机构地区：[1]廊坊师范学院化学与材料科学学院,廊坊065000

出　　处：《无机化学学报》2012年第7期1315-1323,共9页Chinese Journal of Inorganic Chemistry

基　　金：河北省自然科学基金(No.B2010001803);廊坊师范学院科学研究项目重点专项基金(LSZZ201003)资助项目

摘　　要：合成了未见文献报道烟酸分子修饰的自由卟啉o-(niacin)C4O-TPP、p-(niacin)C4O-TPP及锌配合物o-(niacin)C4O-TPPZn、p-(niacin)C4O-TPPZn。通过元素分析、紫外-可见光谱、核磁共振氢谱、红外光谱等多种谱图对结构进行了表征。为模拟金属卟啉的生物功能,采用荧光光谱滴定法测定了金属锌卟啉与人血清白蛋白(HSA)相互作用的光谱性质。按照Stern-Volmer方程、Lineweaver-Burk双倒数方程分析和处理试验数据,得到了反应的猝灭常数、结合常数和热力学参数等。实验结果表明:锌卟啉与人血清白蛋白之间发生了较强的静态荧光猝灭效应,二者之间是以氢键或Van der Waals力结合反应。These new tailed porphyrins o-（niacin）C40-TPP, p-（niacin）C40-TPP and o-（niacin）C40-TPPZn, p-（niacin） C40-TPPZn modified with nicotinic acid were designed, synthesized and characterized by elementary analysis, UV-Vis, 1H NMR and IR spectrum. The fluorescence properties on the interaction between two kinds of Zn porphyrins and human serum albumin were studied by means of fluorescence spectrum in order to simulate biological function of metalloporphyrin. The experimental results showed that there was great quenching interaction between Zn porphyrins and human serum albumin. The quenching type was static quenching. The fluorescence quenching data was analyzed according to Stem-Volmer equation and Lineweaver-Burk double- reciprocal equation. The quenching constant, binding constant K and thermodynamic parameters were obtained. The mechanism of combination reaction between Zn porphyrins and human serum albumin was hydrogen bonding or Van der Waals interaction.

关 键 词：烟酸 锌卟啉 人血清白蛋白 荧光猝灭 

分 类 号：O621.22[理学—有机化学] O621.24[理学—化学]