Pb^(2+)-牛血清白蛋白复合体系中蛋白质二级结构的研究  

Study on the Secondary Structure of Protein in Solution Containing Pb^(2+) and Bovine Serum Albumin

作　　者：张丽[1] 秦德志[1] 杨维春[1] 刘巧茹[1] 王莉[1] 

机构地区：[1]平顶山学院化学化工学院,河南平顶山467000

出　　处：《分析测试学报》2010年第7期721-725,共5页Journal of Instrumental Analysis

基　　金：平顶山学院高层次人才基金资助项目(2008008)

摘　　要：采用紫外光谱、红外光谱和圆二色谱法研究了Pb2+与牛血清白蛋白(BSA)之间的相互作用和蛋白质微观结构的变化。紫外光谱表明,Pb2+与BSA肽链上的CO存在相互作用,并使蛋白质疏水结构的微环境发生变化;红外光谱研究表明,Pb2+与BSA结合位点可能为—OH和—NH基团,利用二阶导、退卷积和谱线拟合技术对蛋白质红外谱图的酰胺Ⅰ带进行处理推测蛋白质二级结构的变化,结果表明蛋白质α螺旋和β折叠二级结构含量降低,β转角二级结构含量增加;圆二色谱(CD)也表明Pb2+与BSA的结合使蛋白质的构象发生了改变。The interaction between Pb2＋ and bovine serum albumin（BSA） has been studied by using ultra-visible spectrum,Fourier transform infrared（FT-IR） spectrum and circular dichroism（CD） spectrum.Results from UV-Vis spectra indicated that Pb2＋reacted with CO group of peptide chains of BSA and resulted in the change of micro-environment of Trp and Tyr residues lyophobic.The spectra and data of FT-IR indicated that Pb2＋ could interact with —OH and —NH groups.The secondary structure contents of BSA,including α-helix,β-sheet,β-turn and random coil were calculated based on the analysis of amide Ⅰ band of FT-IR by second derivative,Fourier self-deconvolution（FSD） and curve-fitting method.Results showed that the contents of α-helix and β-sheet were decreased while that of β-turn was increased,whereas the content of random coil varied scarcely,which was consistent with the results obtained from CD spectra.Therefore,the reaction between Pb ions and BSA could result in the change of BSA conformation by losing its bio-activity,and finally lead to the pathological change in organism.

关 键 词：PB2+ 牛血清白蛋白(BSA) 紫外光谱 红外光谱 圆二色谱 蛋白质 二级结构 

分 类 号：O657.3[理学—分析化学] O629.73[理学—化学]