3-溴丙酮酸与人血清白蛋白相互作用的光谱学研究  

Spectroscopic Studies on Interaction Between 3-Bromopyruvic Acid and Human Serum Albumin

作　　者：裴明砚[1] 郑学仿[1,2] 曹洪玉[1,2] 唐乾[1,2] 

机构地区：[1]辽宁省生物有机化学重点实验室,大连116622 [2]大连大学生物工程学院,大连116622

出　　处：《分析化学》2010年第7期948-952,共5页Chinese Journal of Analytical Chemistry

基　　金：国家自然科学基金(No.20871024);辽宁省优秀人才培养计划项目(No.RC-04-10);辽宁省高校创新团队项目(No.2006T002;2009T003);大连市科技计划项目(No.2008E11SF170)资助

摘　　要：运用荧光光谱、紫外可见吸收光谱和圆二色光谱法研究了抗肿瘤药物3-溴丙酮酸(3-Brom opyruvic acid,3-BrPA)与人血清白蛋白(Human serum albumin,HSA)的相互作用。3-BrPA对HSA的猝灭机制属于静态猝灭,并发生分子间非辐射能量转移。热力学数据显示,二者之间的作用力主要为静电作用;同步荧光光谱表明,3-BrPA与蛋白质中接近色氨酸残基的区域发生了相互作用;荧光光谱研究发现,Zn2+存在时3-BrPA对HSA的猝灭程度进一步增强;圆二色光谱法研究蛋白二级结构结果显示,3-BrPA对HSA的结构影响非常小。The interaction between 3-bromopyruvic acid（3-BrPA） and human serum albumin was studied using fluorescence spectroscopy,synchronous fluorescence spectra,UV/Vis and circular dichroism spectra.Static quenching was predominant between 3-BrPA and HSA,and non-radiation energy transfer between molecules was observed.The results showed that electrostatic force played an important role in the binding reaction.Synchronous fluorescence spectral results revealed that the binding of 3-BrPA induced conformational changes of tyrosine and tryptophan of HSA.3-BrPA mainly interacted with the residues surrounding to the tyrosine.The further quenching phenomenon of the interaction between 3-BrPA and HSA induced by Zn2＋ was investigated with the application of fluorescence spectroscopy.The secondary structure of HSA was studied with the presence of 3-BrPA using CD spectra and the result proved that 3-BrPA had little influence on HSA.

关 键 词：3-溴丙酮酸 人血清白蛋白 相互作用 荧光光谱 紫外可见光谱 圆二色光谱 

分 类 号：R96[医药卫生—药理学]