物理化学学报 >> 2011, Vol. 27 >> Issue (08): 1907-1912.doi: 10.3866/PKU.WHXB20110822

软物质 上一篇    下一篇

血红蛋白在Span 80/PEG 400/H2O囊泡体系中的结构性质

王元有1,2, 华伟1, 刘天晴1   

  1. 1. 扬州大学化学化工学院, 江苏 扬州 225002;
    2. 扬州工业职业技术学院, 江苏 扬州 225127
  • 收稿日期:2011-02-28 修回日期:2011-05-18 发布日期:2011-07-19
  • 通讯作者: 刘天晴 E-mail:tqliu@yzu.edu.cn
  • 基金资助:

    国家自然科学基金(20573091)资助项目

Structural Property of Hemoglobin in Span 80/PEG 400/H2O Niosome System

WANG Yuan-You1,2, HUA Wei1, LIU Tian-Qing1   

  1. 1. School of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou 225002, Jiangsu Province, P. R. China;
    2. Department of Chemical Engineering, Yangzhou Polytechnic Institute, Yangzhou 225127, Jiangsu Province, P. R. China
  • Received:2011-02-28 Revised:2011-05-18 Published:2011-07-19
  • Contact: LIU Tian-Qing E-mail:tqliu@yzu.edu.cn
  • Supported by:

    The project was supported by the National Natural Science Foundation of China (20573091).

摘要:

通过紫外-可见吸收光谱、荧光光谱、动态光散射、圆二色谱、负染-透射电镜(NS-TEM)和冷冻蚀刻-透射电镜(FE-TEM)等实验方法研究了血红蛋白(Hb)与Span 80/PEG 400/H2O囊泡间的相互作用及其结构特性. 结果表明: Hb易于吸附在囊泡表面, 使得囊泡的表观半径稍有增大; Hb的肽链在囊泡表面能够逐渐伸开, 特征荧光峰强度显著增强, 部分氨基酸残基进一步暴露, α-螺旋结构含量减少, β-折叠和β-转角结构含量增加, 无规卷曲结构含量基本不变. 囊泡体系中Hb的稳定性与囊泡的稳定性有关.

关键词: 血红蛋白, 结构, 性质, 非离子囊泡

Abstract:

The structural property of hemoglobin (Hb) was studied in detail by UV-Vis absorption, fluorescence, circular dichroism, negative staining-transmission electron microscopy (NS-TEM), and freeze etching-transmission electron microscopy (FE-TEM) techniques using a Span 80/PEG 400/H2O niosome system. The obtained results show that Hb is adsorbed onto the surface of niosome. The peptide chain of Hb spreads out and the apparent radius of the niosome, the intensities of the UV-Vis absorption peaks, and the fluorescence peaks increase. For the second structural parameter of Hb, the α-helix content decreases but the β-sheet and β-turn content increases. The stability of Hb varies with that of the niosome.

Key words: Hemoglobin, Structure, Property, Niosome

MSC2000: 

  • O648