摘要
以2-(2-氨基苯基)苯并咪唑(L 2)和K 2PtCl 4为原料反应合成铂配合物[Pt(L 2)2Cl 2]·H 2O(L 2-Pt),并获得其晶体结构。在生理条件下(pH 7.40),利用紫外吸收光谱、荧光光谱研究L 2和L 2-Pt对牛血清白蛋白(BSA)相互作用的影响。结果表明,L 2和L 2-Pt通过静态猝灭方式引起BSA荧光发生猝灭,在298、304、310 K这3个温度下,L 2-Pt对BSA的猝灭率及猝灭常数均大于L 2。焓变(ΔH)、熵变(ΔS)和吉布斯自由能变化(ΔG)表明,L 2与BSA间的作用力主要是疏水力(ΔH>0、ΔS>0),结合是自发进行的(ΔG<0);而L 2-Pt与BSA间的作用力主要是氢键和范德华力(ΔH<0、ΔS<0),结合也是自发进行的(ΔG<0)。紫外-可见吸收光谱和同步荧光光谱表明L 2-Pt并未使BSA的微结构发生改变。
The platinum complex[Pt(L 2)2Cl 2]·H 2O(L 2-Pt)was synthesized from 2-(2-aminophenyl)benzimidazole(L 2)and K 2PtCl 4 as raw materials.The corresponding crystal structure was obtained.The effect of L 2 and L 2-Pt to bovine serum albumin(BSA)was studied by UV absorption,fluorescence spectroscopy under physiological conditions(pH 7.4).The results revealed that L 2 and L 2-Pt caused the fluorescence quenching of BSA through a static quenching procedure,and the quenching rate and quenching constants of L 2-Pt on BSA are higher than those of L 2 at 298,304 and 310 K,respectively.The calculating of enthalpy change(ΔH)and the entropy change(ΔS)and gibbs free energy(ΔG)implied that the main interaction force of L 2 with BSA was hydrophobic force(ΔH>0,ΔS>0),and the binding process was spontaneous(ΔG<0).While the main interaction force of L 2-Pt with BSA was hydrogen bonds and van der Waals forces(ΔH<0,ΔS<0),and the binding process also was spontaneous(ΔG<0).The UV-Vis spectroscopy and synchronous fluorescence indicated that L 2-Pt did not alter the microstructure of BSA.
作者
袁涛
覃姣兰
罗翠萍
仇继家
钟雨佳
姚鹏飞
YUAN Tao;QIN Jiao-lan;LUO Cui-ping;QIU Ji-jia;ZHONG Yu-jia;YAO Peng-fei(Guangxi Key Laboratory of Urban Water Environment,College of Chemical and Environmental Engineering,Baise University,Baise 533000,China)
出处
《化学试剂》
CAS
北大核心
2023年第2期62-68,共7页
Chemical Reagents
基金
广西省部共建药用资源化学与药物分子工程国家重点实验室开放课题项目(CMEMR2019-B11)
国家级大学生创新创业训练计划项目(201910609028,教高司函[2020]13号,202010609011)。
关键词
铂配合物
牛血清白蛋白
荧光光谱
相互作用
静态猝灭
platinum complex
bovine serum albumi
fluorescence spectrum
interaction
static quenching