一种新型含硒席夫碱与人血清白蛋白相互作用的研究  

Study on Interaction Between A Novel Schiff Base Containing Selenium and Human Serum Albumin

作　　者：刘洁[1] 刘文举[1] 吴鸣虎[1] 

机构地区：[1]湖北科技学院核技术与化学生物学院,湖北咸宁437100

出　　处：《化学与生物工程》2013年第9期27-31,共5页Chemistry & Bioengineering

基　　金：国家自然科学基金资助项目(21202136)

摘　　要：应用紫外吸收光谱和荧光光谱研究了新型含硒席夫碱2-苄基亚胺基次甲基-4-(3-苄基亚胺基次甲基-4-羟基-苯硒基)苯酚(BBHP)与人血清白蛋白(HSA)之间的相互作用。结果表明,在生理pH值条件下BBHP主要通过形成复合物的静态猝灭方式使HSA的内源荧光得以强烈猝灭;BBHP与HSA主要有1个结合位点数,298K时的结合常数为1.392×106 L·mol-1;该结合反应为自发的放热过程,相互作用力主要为氢键和范德华力。根据Frster无辐射能量转移理论计算了两者之间的结合距离r=2.42nm,同时考察了BBHP对HSA构象的影响。The interaction between 2-（ benzylimino-methylene）-4-[- 3-（ benzylimino-methylene）-4-hydroxy- phenylselanyl-]-phenol（BBHP） and human serum albumin（HSA） was studied by UV absorption spectrum and fluorescence spectrum. The intrinsic fluorescence of HSA was rapidly quenched by BBHP mainly through statie quenching at physiological pH value（7.4）. There was one primary binding site on HSA with a binding constant of 1.392×10^6L·mol^-1 at 298 K. The hydrogen bond and Van der Waas interactions were the predominant forces in the binding process. BBHP was about 2.42 nm far from the tryptopha, which was deduced by the Forster theory of non-radiation energy transfer. The synchronous fluorescence spectra suggested the conformation of HSA was changed in the binding reaction.

关 键 词：含硒席夫碱 2-苄基亚胺基次甲基-4-（3-苄基亚胺基次甲基-4-羟基-苯硒基）苯酚（BBHP） 人血清白蛋白 紫外吸收光谱 荧光光谱 

分 类 号：O657.3[理学—分析化学]