布南色林与人血清白蛋白相互作用的光谱学研究  被引量:2

Spectroscopic investigation of interaction between blonanserin and human serum albumin

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作  者:王腾[1] 何晓囡[1] 董颖[2] 张志红[1] 郭晓燕[1] 相秉仁[2] 

机构地区:[1]北京石油化工学院制药工程系,北京102617 [2]中国药科大学分析测试中心,南京210009

出  处:《分析试验室》2012年第1期105-109,共5页Chinese Journal of Analysis Laboratory

基  金:北京石油化工学院URT项目(2010J00139)资助

摘  要:采用荧光光谱研究了模拟生理条件下抗精神病药布南色林与人血清白蛋白的相互作用,结果表明,布南色林对人血清白蛋白的内源性荧光具有猝灭作用且猝灭方式为静态猝灭。布南色林与人血清白蛋白形成了1:1的复合物,结合常数K=1.80×104L/mol,且金属离子对结合反应具有较显著的影响。根据不同温度下的热力学函数确定了布南色林与人血清白蛋白的相互作用力类型以氢键和范德华力为主。同步荧光光谱和傅立叶变换红外光谱表明布南色林对人血清白蛋白二级结构的含量产生影响,α-螺旋和β-折叠的含量降低,β-转角和无卷曲规则的含量明显升高。Fluorescence spectroscopy was used to investigate the interactions of human serum albumin and blonanserin.From the spectra obtained,it was observed that blonanserin had a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure.A complex of blonanserin-HSA was formed with molar ratio of 1:1 and the binding constant K=1.80×104L/mol.From thermodynamic parameters,it can be verified that the binding force between blonanserin and HSA is mainly hydrogen bond and Van der Waals force.The synchronous fluorescence and FT-IR spectra of blonanserin-HSA system also indicated that the presence of blonanserin would change the conformation and the secondary structure of HSA,in which the contents of α-helix and β-sheet structure were decreased,while those of β-turn and random coil structure were increased.

关 键 词:布南色林 人血清白蛋白 荧光光谱 傅立叶变换红外光谱 

分 类 号:O657.3[理学—分析化学]

 

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