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作 者:谢幸秦 XIE Xingqin(Department of Metallurgy and Resource Engineering,Nanning Campus,Guilin University of Technology,Chongzuo,Guangxi 532100,China)
机构地区:[1]桂林理工大学南宁分校-冶金与资源工程系,广西崇左532100
出 处:《应用化学》2020年第5期604-610,共7页Chinese Journal of Applied Chemistry
基 金:广西高校青年教师基础能力提升项目(2019KY0288)资助。
摘 要:在生理条件下,利用紫外-可见光谱和荧光光谱分别研究氨基硫脲芳基铱抗癌物与牛血清蛋白的相互作用。确定作用机制,讨论结合力类型,并研究共存离子对结合常数的影响。实验结果表明,间甲氧基苯甲醛4-苯基-3-氨基硫脲芳基铱(TSC-Ir-6)配合物对牛血清白蛋白(BSA)的内源性荧光有猝灭作用,其猝灭类型为静态猝灭;通过计算二者相互作用时的热力学参数,其结果表明TSC-Ir-6与BSA的结合是一个自发过程(ΔG<0),且体系ΔH<0,ΔS<0,其相互作用力类型为氢键和范德华力,结合位点约为1。共存离子的存在使TSC-Ir-6与BSA之间的结合常数明显增大,结合力更强,提高了其在血浆中的滞留时间,可能得到更好的治疗效果。In this paper,the interaction between thiourea aryl iridium and bovine serum albumin(BSA)was studied by ultraviolet-visible spectroscopy(UV-Vis)and fluorescence spectroscopy under physiological conditions.The mechanism of action was determined,the type of binding force was discussed,and the activation energy of the reaction of thiourea aryl iridium anticancer compound with bovine serum albumin was calculated.The experimental results show that m-methoxybenzaldehyde 4-phenyl-3-thiourea aryl iridium(TSC-Ir-6)complex has a quenching effect on endogenous fluorescence of bovine serum albumin,and the quenching type is static quenching.Through the fixed Stern-Volmer equations and apparent binding constant,the thermodynamic parameters calculated by the formula,it is concluded that the combination of TSC-Ir-6 and BSA is a spontaneous process(ΔG<0),and the interaction forces are hydrogen bonding and van der Waals force.The number of binding sites is about one.With the presence of coexisting ions,the binding constant between TSC-Ir-6 and BSA is significantly increased,the binding force is stronger,and the retention time of TSC-Ir-6 in plasma is improved,which may lead to a better therapeutic effect.
关 键 词:氨基硫脲芳基铱配合物 牛血清蛋白 紫外-可见光谱法 荧光光谱法 相互作用
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