摘要
目的研究肼黄与人血清白蛋白(human serum albumin,HSA)间的结合性质。方法采用荧光淬灭法对肼黄与人血清白蛋白间相互作用进行研究。结果肼黄可以使人血清白蛋白的内源荧光发生淬灭现象。肼黄与人血清白蛋白相互作用的热力学参数计算结果为ΔG0<0、ΔH0<0、ΔS0>0。华法林的加入可使人血清白蛋白-肼黄体系的荧光强度明显降低。结论肼黄以形成人血清白蛋白-肼黄复合物的静态淬灭机制与人血清白蛋白发生相互作用。二者形成人血清白蛋白-肼黄复合物的过程是自发进行的,疏水作用力和氢键在形成人血清白蛋白-肼黄复合物的过程中发挥主要作用。肼黄在人血清白蛋白上的结合位点是与华法林相同的siteⅠ位。
Objective To study the binding properties between tartrazine and human serum albumin( HSA).Methods Fluorescence quenching method was used to study the interaction between tartrazine and HSA.Results Tartrazine could quench the intrinsic fluorescence of HSA obviously. The calculated results of thermodynamic parameters of the interaction between tartrazine and HSA were ΔG0< 0,ΔH0< 0 and ΔS0> 0. The fluorescence intensity of HSA-tartrazine system decreased obviously with the addition of warfarin.Conclusion The fluorescence quenching mechanism was static quenching due to the formation of HSA-tartrazine complex.The formation of HSA-tartrazine complex was spontaneous.The hydrophobic forces and hydrogen bonds played major roles in the interaction between HSA and tartrazine.The binding site of tartrazine on HSA was site I,which is the same as warfarin.
作者
周玲玲
吴春梅
王晓芳
徐亮
刘彬
王新
ZHOU Lingling;WU Chunmei;WANG Xiaofang;XU Liang;LIU Bin;WANG Xin(School of Pharmaceutical Sciences,Liaoning University,Shengyang 110036,China)
出处
《药学研究》
CAS
2018年第12期687-689,704,共4页
Journal of Pharmaceutical Research
基金
国家自然科学基金资助项目(No.21402125)
辽宁大学"大学生创新创业训练计划"项目(No.x201810140280)
