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作 者:李春艳[1] 阮冠宇[2] 单丽[1] 陈锦灿[3] 黄明东[3]
机构地区:[1]福建医科大学药学院,福州350004 [2]福建省妇幼保健院药剂科,福州350001 [3]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,福州350002
出 处:《福建医科大学学报》2010年第4期244-248,共5页Journal of Fujian Medical University
基 金:国家自然科学杰出青年基金(30625011);国家高技术研究发展计划(863计划;2006A02A313)
摘 要:目的研究新型光敏剂五聚赖氨酸-2-羰基酞菁锌(ZnPc-(Lys)5)与牛血清白蛋白(BSA)之间的相互作用。方法从BSA角度采用荧光光谱法和紫外可见光谱法通过荧光猝灭实验探讨ZnPc-(Lys)5与BSA相互作用的猝灭机制、结合常数及结合位点;从ZnPc-(Lys)5角度采用胶束荧光增敏法测定ZnPc-(Lys)5浓度通过Scatchard方程计算ZnPc-(Lys)5与BSA相互作用的结合常数和结合位点数。结果荧光猝灭实验结果表明ZnPc-(Lys)5对BSA的荧光有强烈的猝灭作用,猝灭机制主要是静态猝灭形成基态配合物。不同温度(298,303,308,313,318 K)的结合常数K1分别为12.1×104L/mol,7.69×104L/mol,6.12×104L/mol,4.57×104L/mol,3.76×104L/mol,结合位点数分别为0.93,1.02,1.07,1.13,1.17。Scatchard方程计算出298 K结合常数K2为1.557×105L/mol,结合位点数位1.07。结论从两个方面计算的结合常数和结合位点数基本一致,ZnPc-(Lys)5与血清白蛋白之间主要通过形成基态配合物的方式相互作用,进入血清白蛋白中1个结合位点。Objective To investigate the interaction of pentalysine β-carbonyl-phthalocyanine zinc(ZnPc-(Lys)5) with bovine serum albumin(BSA) by two methods.Methods From the point of BSA,the quenching mechanism,binding constants and sites of the interaction between ZnPc-(Lys)5 and BSA was investigated through the fluorescence quenching experiment by fluorescence spectrometry and UV-visible spectroscopy.From the point of ZnPc-(Lys)5,the constants and sites of the interaction were calculated through micellar enhanced spectrofluorometric determination of ZnPc-(Lys)5 concentration with Scatchard equation.Results The mechanism of fluorescence quenching is static quenching process.The binding constants and the number of binding sites were calculated at different temperatures(298,303,308,313,318 K): 12.1,7.69,6.12,4.57,3.76×104 L/mol and 0.93,1.02,1.07,1.13,1.17,respectively.The binding constant and the number of binding sites calculated from Scatchard equation at 298 K were 1.557×105 L/mol and 1.07,respectively.Conclusion The two methods produce approximately identical data of the binding constant and sites.The results indicate that ZnPc-(Lys)5 strongly binds to BSA at a molar ratio of 1∶1.
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